Updated on 2025/02/16

写真a

 
SUZUKI Kazushi
 
Organization
Academic Assembly Institute of Science and Technology NOUGAKU KEIRETSU Professor
Faculty of Agriculture Professor
Title
Professor
External link

Degree

  • 博士(農学) ( 1999.3   新潟大学 )

Research Areas

  • Life Science / Applied microbiology

Research History (researchmap)

  • Niigata University   Sakeology Center   Director

    2020.1 - 2023.3

      More details

  • Niigata University   Graduate School of Science and Technology Life and Food Sciences   Professor

    2018.4

      More details

  • Niigata University   Faculty of Agriculture   Professor

    2018.4

      More details

  • Niigata University   Faculty of Agriculture Department of Agriculture   Associate Professor

    2017.4 - 2018.3

      More details

  • Niigata University   Graduate School of Science and Technology Life and Food Sciences   Associate Professor

    2006.7 - 2018.3

      More details

  • Niigata University   Faculty of Agriculture Department of Applied Biological Chemistry   Associate Professor

    2006.7 - 2017.3

      More details

▶ display all

Research History

  • Niigata University   Faculty of Agriculture   Professor

    2018.4

  • Niigata University   Faculty of Agriculture Department of Agriculture   Associate Professor

    2017.4 - 2018.3

  • Niigata University   Graduate School of Science and Technology Life and Food Sciences   Associate Professor

    2006.7 - 2018.3

  • Niigata University   Graduate School of Science and Technology Life and Food Sciences   Associate Professor

    2006.7 - 2018.3

  • Niigata University   Faculty of Agriculture Department of Applied Biological Chemistry   Associate Professor

    2006.7 - 2017.3

Professional Memberships

▶ display all

 

Papers

  • Complete genome sequence of Serratia plymuthica SWSY-3.47. Reviewed International journal

    Himari Takahashi, Tomoro Warashina, Yui Takahashi, Mayuki Tanaka, Kazushi Suzuki, Teppei Morita, Kazuharu Arakawa

    Microbiology resource announcements   e0081524   2024.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Serratia plymuthica strain SWSY-3.47 is a Gram-negative, rod-shaped bacteria isolated for its high chitinolytic activity. Here, we report the complete genome of this strain comprised of a single circular chromosome of 5,636,345 bp with a G + C content of 56.0%.

    DOI: 10.1128/mra.00815-24

    PubMed

    researchmap

  • Unfolding of the bacterial fibronectin type III domains from family 18 glycoside hydrolases Reviewed

    Taro OTAGAKI, Ayane NAKAJIMA, Kazushi SUZUKI, Hayuki SUGIMOTO

    Chitin Chitosan Research   30 ( 1 )   9 - 19   2024

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    researchmap

  • Identification of the Csr global regulatory system mediated by small RNA decay in Aeromonas salmonicida Reviewed

    Olga Gladyshchuk, Masaki Yoshida, Koume Togashi, Hayuki Sugimoto, Kazushi Suzuki

    The Journal of General and Applied Microbiology   70 ( 1 )   n/a - n/a   2024

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Microbiology Research Foundation  

    We investigated the presence and functionality of the carbon storage regulator (Csr) system in Aeromonas salmonicida SWSY-1.411. CsrA, an RNA-binding protein, shared 89% amino acid sequence identity with Escherichia coli CsrA. CsrB/C sRNAs exhibited a typical stem-loop structure, with more GGA motifs, which bind CsrA, than E. coli. CsrD had limited sequence identity with E. coli CsrD; however, it contained the conserved GGDEF and EAL domains. Functional analysis in E. coli demonstrated that the Csr system of A. salmonicida influences glycogen biosynthesis, biofilm formation, motility, and stability of both CsrB and CsrC sRNAs. These findings suggest that in A. salmonicida, the Csr system affects phenotypes like its E. coli counterpart. In A. salmonicida, defects in csr homologs affected biofilm formation, motility, and chitinase production. However, glycogen accumulation and protease production were unaffected. The expression of flagellar-related genes and chitinase genes was suppressed in the csrA-deficient A. salmonicida. Northern blot analysis indicated the stabilization of CsrB and CsrC in the csrD-deficient A. salmonicida. Similar to that in E. coli, the Csr system in A. salmonicida comprises the RNA-binding protein CsrA, the sRNAs CsrB and CsrC, and the sRNA decay factor CsrD. This study underscores the conservation and functionality of the Csr system and raises questions about its regulatory targets and mechanisms in A. salmonicida.

    DOI: 10.2323/jgam.2023.12.004

    PubMed

    researchmap

  • Chitinase system of Aeromonas salmonicida, and characterization of enzymes involved in chitin degradation. Reviewed International journal

    Iuliia Pentekhina, Tatsuyuki Hattori, Dinh Minh Tran, Mizuki Shima, Takeshi Watanabe, Hayuki Sugimoto, Kazushi Suzuki

    Bioscience, biotechnology, and biochemistry   84 ( 9 )   1936 - 1947   2020.9

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    The genes encoding chitin-degrading enzymes in Aeromonas salmonicida SWSY-1.411 were identified and cloned in Escherichia coli. The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC and AsChiD, and an auxiliary activities family 10 protein, lytic polysaccharide monooxygenase: AsLPMO10A. These enzymes were successfully expressed in E. coli and purified. AsChiB had the highest hydrolytic activity against insoluble chitin. AsChiD had the highest activity against water-soluble chitin. The peroxygenase activity of AsLPMO10A was lower compared to SmLPMO10A from Serratia marcescens. Synergism on powdered chitin degradation was observed when AsChiA and AsLPMO10A were combined with other chitinases of this strain. More than twice the increase of the synergistic effect was observed when powdered chitin was treated by a combination of AsLPMO10A with all chitinases. GH19 chitinases suppressed the hyphal growth of Trichoderma reesei.

    DOI: 10.1080/09168451.2020.1771539

    PubMed

    researchmap

  • Unfolding of CBP21, a lytic polysaccharide monooxygenase, without dissociation of its copper ion cofactor. Reviewed

    Sugimoto H, Nakajima Y, Motoyama A, Katagiri E, Watanabe T, Suzuki K

    Biopolymers   111 ( 1 )   e23339   2019.11

     More details

    Publishing type:Research paper (scientific journal)   Publisher:Wiley  

    DOI: 10.1002/bip.23339

    PubMed

    researchmap

    Other Link: https://onlinelibrary.wiley.com/doi/full-xml/10.1002/bip.23339

  • Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis. Reviewed International journal

    Akihiko Nakamura, Tomoyuki Tasaki, Yasuko Okuni, Chihong Song, Kazuyoshi Murata, Toshiya Kozai, Mayu Hara, Hayuki Sugimoto, Kazushi Suzuki, Takeshi Watanabe, Takayuki Uchihashi, Hiroyuki Noji, Ryota Iino

    Physical chemistry chemical physics : PCCP   20 ( 5 )   3010 - 3018   2018.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Serratia marcescens chitinase A is a linear molecular motor that hydrolyses crystalline chitin in a processive manner. Here, we quantitatively determined the rate constants of elementary reaction steps, including binding (kon), translational movement (ktr), and dissociation (koff) with single-molecule fluorescence imaging. The kon for a single chitin microfibril was 2.1 × 109 M-1 μm-1 s-1. The koff showed two components, k (3.2 s-1, 78%) and k (0.38 s-1, 22%), corresponding to bindings to different crystal surfaces. From the kon, k, k and ratio of fast and slow dissociations, dissociation constants for low and high affinity sites were estimated as 2.0 × 10-9 M μm and 8.1 × 10-10 M μm, respectively. The ktr was 52.5 nm s-1, and processivity was estimated as 60.4. The apparent inconsistency between high turnover (52.5 s-1) calculated from ktr and biochemically determined low kcat (2.6 s-1) is explained by a low ratio (4.8%) of productive enzymes on the chitin surface (52.5 s-1 × 0.048 = 2.5 s-1). Our results highlight the importance of single-molecule analysis in understanding the mechanism of enzymes acting on a solid-liquid interface.

    DOI: 10.1039/c7cp04606e

    PubMed

    researchmap

  • Correction: Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis. Reviewed

    Nakamura A, Tasaki T, Okuni Y, Song C, Murata K, Kozai T, Hara M, Sugimoto H, Suzuki K, Watanabe T, Uchihashi T, Noji H, Iino R

    Physical chemistry chemical physics : PCCP   20 ( 5 )   3844 - 3844   2018.1

     More details

    Language:English   Publisher:ROYAL SOC CHEMISTRY  

    DOI: 10.1039/c8cp90024h

    Web of Science

    PubMed

    researchmap

  • Identification and characterization of chitinolytic bacteria isolated from a freshwater lake Reviewed

    Dinh Minh Tran, Hayuki Sugimoto, Dzung Anh Nguyen, Takeshi Watanabe, Kazushi Suzuki

    Bioscience, Biotechnology and Biochemistry   82 ( 2 )   343 - 355   2018

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Japan Society for Bioscience Biotechnology and Agrochemistry  

    To develop a novel type of biocontrol agent, we focus on bacteria that are characterized by both chitinase activity and biofilm development. Chitinolytic bacteria were isolated from sediments and chitin flakes immersed in the water of a sand dune lake, Sakata, in Niigata, Japan. Thirty-one isolates from more than 5100 isolated strains were examined chitinase activity and biofilm formation. Phylogenetic analysis of these isolates based on the 16S rRNA gene sequences revealed that most isolates belonged to the family Aeromonadaceae, followed by Paenibacillaceae, Enterobacteriaceae, and Neisseriaceae. The specific activity of chitinase of four selected strains was higher than that of a reference strain. The molecular size of one chitinase produced by Andreprevotia was greater than that of typical bacterial chitinases. The dialyzed culture supernatant containing chitinases of the four strains suppressed hyphal growth of Trichoderma reesei. These results indicate that these four strains are good candidates for biocontrol agents.

    DOI: 10.1080/09168451.2017.1422969

    Scopus

    PubMed

    researchmap

  • Antagonistic control of the turnover pathway for the global regulatory sRNA CsrB by the CsrA and CsrD proteins Reviewed

    Christopher A. Vakulskas, Yuanyuan Leng, Hazuki Abe, Takumi Amaki, Akihiro Okayama, Paul Babitzke, Kazushi Suzuki, Tony Romeo

    NUCLEIC ACIDS RESEARCH   44 ( 16 )   7896 - 7910   2016.9

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:OXFORD UNIV PRESS  

    The widely conserved protein CsrA (carbon storage regulator A) globally regulates bacterial gene expression at the post-transcriptional level. In many species, CsrA activity is governed by untranslated sRNAs, CsrB and CsrC in Escherichia coli, which bind to multiple CsrA dimers, sequestering them from lower affinity mRNA targets. Both the synthesis and turnover of CsrB/C are regulated. Their turnover requires the housekeeping endonuclease RNase E and is activated by the presence of a preferred carbon source via the binding of EIIA(Glc) of the glucose transport system to the GGDEF-EAL domain protein CsrD. We demonstrate that the CsrB 3' segment contains the features necessary for CsrD-mediated decay. RNase E cleavage in an unstructured segment located immediately upstream from the intrinsic terminator is necessary for subsequent degradation to occur. CsrA stabilizes CsrB against RNase E cleavage by binding to two canonical sites adjacent to the necessary cleavage site, while CsrD acts by overcoming CsrA-mediated protection. Our genetic, biochemical and structural studies establish a molecular framework for sRNA turnover by the CsrD-RNase E pathway. We propose that CsrD evolution was driven by the selective advantage of decoupling Csr sRNA decay from CsrA binding, connecting it instead to the availability of a preferred carbon source.

    DOI: 10.1093/nar/gkw484

    Web of Science

    PubMed

    researchmap

  • Regulation of chitinase system by small RNA in Serratia marcescens

    K. Suzuki, H. Sugimoto, T. Watanabe

    Proceeding of the 6th international symposium for the development of integrated pest management (IPM) in Asia and Africa 2016   22 ( 2 )   77 - 82   2016.5

     More details

    Language:English  

    J-GLOBAL

    researchmap

  • Screening of chitinolytic bacteria by measuring chitinase activity and biofilm formation.

    D. M. Tran, H. Sugimoto, T. Watanabe, K. Suzuki

    Proceeding of the 6th international symposium for the development of integrated pest management (IPM) in Asia and Africa 2016   83 - 87   2016.5

     More details

    Language:English  

    researchmap

  • Suppressive effects of Bacillus spp. on mycelia, apothecia and sclerotia formation of Sclerotinia sclerotiorum and potential as biological control of white mold on mustard Reviewed

    Md Muzahid E. Rahman, Delwar M. Hossain, Kazuki Suzuki, Ayaka Shiiya, Kazushi Suzuki, Tapan Kumar Dey, Masanori Nonaka, Naoki Harada

    AUSTRALASIAN PLANT PATHOLOGY   45 ( 1 )   103 - 117   2016.2

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER  

    Biological control, especially with Bacillus-based biocontrol agents, offers an attractive alternative to synthetic pesticides for sustainable management of white mold disease caused by Sclerotinia sclerotiorum. In this study, eight effective Bacillus isolates were isolated from rhizospheric soil samples as potential bacterial biocontrol agents. Cultural, biochemical, and molecular analyses of 16S rDNA and gyrase subunit A (gyrA) confirmed that all isolates were identified as Bacillus amyloliquefaciens subsp. plantarum. The production of hydrolytic enzymes and the plant growth-promotional attributes of these isolates confirmed their multifaceted potential. Molecular analysis of the eight biosynthetic genes, which are related to antibiotic properties of bacilli, revealed that all of the isolates possess five genes: bacA for bacilysin, dfnM for difficidin, fenA for fengycin, ituA for iturin, and sfp for surfactin. The Bacillus isolates inhibited mycelial growth and suppressed formation of sclerotia during an in vitro test against S. sclerotiorum. Deformities and cell-wall lysis of mycelia, abnormalities of apothecia, and germination failure of ascospores through interaction with the Bacillus isolates were observed with light and scanning electron microscopes, suggesting that they have high antagonistic effects against S. sclerotiorum. Seed bacterization with the Bacillus isolates protected mustard seedlings in vitro up to 98 % against S. sclerotiorum. In a pot experiment, damages of mustard plants against the pathogen decreased up to 90 % after foliar spray of the Bacillus isolates. In addition, the isolates increased seed germination and accelerated seedling vigor of mustard, suggesting that they have plant growth-promoting functions.

    DOI: 10.1007/s13313-016-0397-4

    Web of Science

    researchmap

  • Regulation of the chitin degradation and utilization system by the ChiX small RNA in Serratia marcescens 2170 Reviewed

    Kazushi Suzuki, Mari Shimizu, Naomi Sasaki, Chisana Ogawa, Haruka Minami, Hayuki Sugimoto, Takeshi Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   80 ( 2 )   376 - 385   2016.2

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    Serratia marcescens 2170 produces three different types of chitinases and chitin-binding protein CBP21. We found that transposon insertion into the 5 untranslated region (5 UTR) of chiPQ-ctb led to defective chitinase and CBP21 production. ChiX small RNA possessed the complementary sequence of the 5 UTRs of the chiPQ-ctb and chiR and repressed the expression of chiP and chiR. ChiX was detected in a medium containing glucose, glycerol, GlcNAc, and (GlcNAc)(2), but the expression of both chiP and chiR was only observed in a medium containing (GlcNAc)(2). chiX mutant produced chitinases, CBP21, and chitobiase without induction. chiP transcripts were more abundant than those of chiR or chiX in a medium containing (GlcNAc)(2). These results suggest that the constitutively expressed ChiX binds to the highly abundant chiP 5 UTR, thereby leading to the induction of chiR mRNA translation and the subsequent expression of chitinases and CBP21.

    DOI: 10.1080/09168451.2015.1083399

    Web of Science

    PubMed

    researchmap

  • Analysis of subfamily C chitinases in bacterial glycoside hydrolase family 18 Reviewed

    鈴木一史, 鈴木一史, 杉本華幸, 杉本華幸, 工藤江利子, 伊藤学, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   21 ( 3 )   209 - 218   2015.11

     More details

  • Construction of a CBP21-defective mutant of Serratia marcescens 2170 Reviewed

    桜井大地, 杉本華幸, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   21 ( 2 )   46 - 51   2015.7

     More details

  • Differences in the roles of the two surface-exposed tyrosine residues, Y240 and Y481, of Serratia marcescens chitinase B during processive degradation of crystalline chitin Reviewed

    Hayuki Sugimoto, Keita Nakamura, Yuji Nishino, Yuta Idezawa, Akiko Fujinuma, Kazushi Suzuki, Takeshi Watanabe

    JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY   61 ( 6 )   255 - 261   2015

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:MICROBIOL RES FOUNDATION  

    Chitinase B from Serratia marcescens 2170 is one of the processive chitinases, and it has a linear path of aromatic amino acid residues on the surface and in the catalytic cleft. There are four surface-exposed residues lined-up towards the cleft, Y481, W479, W252, and Y240. The substitution of these residues with alanine causes a decrease in both the extent of the substrate binding and the hydrolytic activity (Katouno et al., 2004). Here, we examine the three mutants without losing the substrate-binding ability, Y240W, Y481W, and Y240W/Y481W. These mutants were prepared for a detailed analysis of the functions of Y240 and Y481, which showed a lower contribution to substrate binding than W479 and W252. The parameters for the binding of the three mutants to crystalline beta-chitin were similar to those for the wild type. The hydrolytic activity of Y240W and Y240W/Y481W against crystalline beta-chitin was significantly decreased. However, the hydrolytic activity of Y481W was similar to that of the wild type, indicating some differences in the roles of Y240 and Y481 during the processive degradation of crystalline beta-chitin. Taken together with the previous results, it was suggested that while Y240 and Y481 were required for the substrate binding, Y240 had additional roles in the processive degradation of crystalline beta-chitin, possibly in guiding a chitin chain into the catalytic cleft.

    DOI: 10.2323/jgam.61.255

    Web of Science

    PubMed

    researchmap

  • Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin Reviewed

    Kiyohiko Igarashi, Takayuki Uchihashi, Taku Uchiyama, Hayuki Sugimoto, Masahisa Wada, Kazushi Suzuki, Shohei Sakuda, Toshio Ando, Takeshi Watanabe, Masahiro Samejima

    NATURE COMMUNICATIONS   5   3975   2014.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATURE PUBLISHING GROUP  

    Processivity refers to the ability of synthesizing, modifying and degrading enzymes to catalyse multiple successive cycles of reaction with polymeric substrates without disengaging from the substrates. Since biomass polysaccharides, such as chitin and cellulose, often form recalcitrant crystalline regions, their degradation is highly dependent on the processivity of degrading enzymes. Here we employ high-speed atomic force microscopy to directly visualize the movement of two processive glycoside hydrolase family 18 chitinases (ChiA and ChiB) from the chitinolytic bacterium Serratia marcescens on crystalline beta-chitin. The half-life of processive movement and the velocity of ChiA are larger than those of ChiB, suggesting that asymmetric subsite architecture determines both the direction and the magnitude of processive degradation of crystalline polysaccharides. The directions of processive movements of ChiA and ChiB are observed to be opposite. The molecular mechanism of the two-way traffic is discussed, including a comparison with the processive cellobiohydrolases of the cellulolytic system.

    DOI: 10.1038/ncomms4975

    Web of Science

    PubMed

    researchmap

  • Construction and basic characterization of deletion mutants of the genes involved in chitin utilization by Serratia marcescens 2170 Reviewed

    Shinya Takanao, Syouta Honma, Takuma Miura, Chisana Ogawa, Hayuki Sugimoto, Kazushi Suzuki, Takeshi Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   78 ( 3 )   524 - 532   2014

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    In order to elucidate the roles of ChiP, ChiQ, and ChiX in chitin utilization by Serratia marcescens 2170, the construction of single-gene deletion mutants of the chiP, chiQ, and chiX genes was attempted by allelic exchange mutagenesis. Delta chiP formed smaller clearing zones and Delta chiX formed larger ones than wild-type 2170 on an agar plate containing colloidal chitin. Delta chiP grew slowly on the lower concentration of (GlcNAc)(2), and there was essentially no growth on chitin oligosaccharides larger than (GlcNAc)(3). The gene product of chiP was detected in the outer membrane fraction, consistently with the hypothesis that chiP encodes outer membrane chitoporin. Deletion of chiQ decreased and that of chiX increased the growth rates on chitin oligosaccharides. These observations strongly suggest that all three genes are involved in chitin utilization and that the deletion mutants obtained in this study might prove useful tools to clarify the details of the chitin utilization system of this bacterium.

    DOI: 10.1080/09168451.2014.882755

    Web of Science

    PubMed

    researchmap

  • Identification of a Csr system in Serratia marcescens 2170 Reviewed

    Manabu Ito, Kazuki Nomura, Hayuki Sugimoto, Takeshi Watanabe, Kazushi Suzuki

    JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY   60 ( 2 )   79 - 88   2014

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:MICROBIOL RES FOUNDATION  

    The carbon storage regulator (Csr) global regulatory system is conserved in many eubacteria and coordinates the expression of various genes that facilitate adaptation during the major physiological growth phase. The Csr system in Escherichia coli comprises an RNA-binding protein, CsrA; small non-coding RNAs, CsrB and CsrC; and a decay factor for small RNAs, CsrD. In this study, we identified the Csr system in Serratia marcescens 2170. S. marcescens CsrA was 97% identical to E. coli CsrA. CsrB and CsrC RNAs had typical stem-loop structures, including a GGA motif that is the CsrA binding site. CsrD was composed of N-terminal two times transmembrane region and HAMP-like, GGDEF, and EAL domains. Overexpression of S. marcescens csr genes complemented the phenotype of E. coli csr mutants. S. marcescens CsrD affected the decay of CsrB and CsrC RNAs in E. coli. These results suggest that the Csr system in S. marcescens is composed of an RNA-binding protein, two Csr small RNAs, and a decay factor for Csr small RNAs.

    DOI: 10.2323/jgam.60.79

    Web of Science

    PubMed

    researchmap

  • Involvement of Gln679, in addition to Trp687, in chitin-binding activity of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 Reviewed

    Masashi Hara, Hayuki Sugimoto, Michio Uemura, Ken-ichi Akagi, Kazushi Suzuki, Takahisa Ikegami, Takeshi Watanabe

    JOURNAL OF BIOCHEMISTRY   154 ( 2 )   185 - 193   2013.8

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:OXFORD UNIV PRESS  

    Chitinase A1 (ChiA1) from Bacillus circulans WL-12 comprises an N-terminal catalytic domain, two fibronectin type III domains, and a C-terminal chitin-binding domain (ChBD). The ChBD of ChiA1 (ChBD(ChiA1)) belongs to carbohydrate-binding module (CBM) family 12 and specifically binds to insoluble or crystalline chitin. It has been suggested that tryptophan-687 (Trp687) is involved in the chitin-binding activity of this ChBD. Site-directed mutagenesis was used to identify additional amino acid residues required for chitin-binding activity of this domain. Furthermore, a total of 14 amino acid residues in ChBD(ChiA1) were carefully selected, and it was found that mutation of Gln679, which is not well-conserved in CBM family 12, significantly decreased the binding activity to colloidal chitin. A nuclear magnetic resonance study demonstrated that neither the Q679A nor the W687A mutation altered the overall structure of ChBD(ChiA1). Therefore, Gln679 was identified as a new residue that is involved in the chitin-binding activity of ChBD(ChiA1) in addition to Trp687. However, the mechanism of chitin binding by ChBD is still unknown.

    DOI: 10.1093/jb/mvt043

    Web of Science

    PubMed

    researchmap

  • Regulation of chitinase system in Serratia marcescens

    K. Suzuki, M. Shimizu, N. Sasaki, T. Watanabe

    Proceedings of the 9th asia pacific chitin and chitosan symposium   16 ( 2 )   127 - 131   2012.12

     More details

    Language:English  

    J-GLOBAL

    researchmap

  • Regulation of Chitinase Production by the 5 '-Untranslated Region of the ybfM in Serratia marcescens 2170 Reviewed

    Tadayuki Toratani, Kazushi Suzuki, Mari Shimizu, Hayuki Sugimoto, Takeshi Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   76 ( 10 )   1920 - 1924   2012.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    Serratia marcescens 2170 produces three chitinases and the chitin-binding protein CBP21, and efficiently degrades insoluble and crystalline chitin. The three chitinases and CBP21 are induced by N,N'-diacetylchitobiose [(GlcNAc)(2)], the major product of chitin hydrolysis by S. marcescens chitinases. We have found that uptake of both (GlcNAc)(2) and N-acetylglucosamine (GlcNAc) is important for the efficient utilization of (GlcNAc)(2) because (GlcNAc)(2) is less efficiently fermented by S. marcescens 2170 in the absence of chitobiase. In order to determine the mechanism of utilization of the degradation products of chitin by S. marcescens, chitobiase deficient transposon mutants were screened. A transposon present in chitobiase-deficient mutants was inserted into the ybfMN-ctb cluster. The mutants produced chitinases, except for TT327, in which a transposon was inserted into the 5'-untranslated region (5'-UTR) of ybfM. Ectopic expression of this region in TT327 restored chitinase production. These results indicate that the 5'-UTR of ybfM is important for chitinase induction in S. marcescens.

    DOI: 10.1271/bbb.120403

    Web of Science

    PubMed

    researchmap

  • Serratia marcescens Induces Apoptotic Cell Death in Host Immune Cells via a Lipopolysaccharide- and Flagella-dependent Mechanism Reviewed

    Kenichi Ishii, Tatsuo Adachi, Katsutoshi Imamura, Shinya Takano, Kimihito Usui, Kazushi Suzuki, Hiroshi Hamamoto, Takeshi Watanabe, Kazuhisa Sekimizu

    JOURNAL OF BIOLOGICAL CHEMISTRY   287 ( 43 )   36582 - 36592   2012.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

    Injection of Serratia marcescens into the blood (hemolymph) of the silkworm, Bombyx mori, induced the activation of c-Jun NH2-terminal kinase (JNK), followed by caspase activation and apoptosis of blood cells (hemocytes). This process impaired the innate immune response in which pathogen cell wall components, such as glucan, stimulate hemocytes, leading to the activation of insect cytokine paralytic peptide. S. marcescens induced apoptotic cell death of silkworm hemocytes and mouse peritoneal macrophages in vitro. We searched for S. marcescens transposon mutants with attenuated ability to induce apoptosis of silkworm hemocytes. Among the genes identified, disruption mutants of wecA (a gene involved in lipopolysaccharide O-antigen synthesis), and flhD and fliR (essential genes in flagella synthesis) showed reduced motility and impaired induction of mouse macrophage cell death. These findings suggest that S. marcescens induces apoptosis of host immune cells via lipopolysaccharide- and flagella-dependent motility, leading to the suppression of host innate immunity.

    DOI: 10.1074/jbc.M112.399667

    Web of Science

    PubMed

    researchmap

  • Mechanism of crystalline chitin hydrolysis by a unique enzyme, Serratia marcescens chitinase B Reviewed

    藤沼晶子, 丸屋良輔, 杉本華幸, 中村啓太, 橋詰義夫, 五十嵐圭日子, 鮫島正浩, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   18 ( 2 )   148 - 149   2012.7

     More details

  • Loss of Aspergillus oryzae amyR function indirectly affects hemicellulolytic and cellulolytic enzyme production Reviewed

    Jun Watanabe, Hisaki Tanaka, Yoshinobu Mogi, Tatsuo Yamazaki, Kazushi Suzuki, Takeshi Watanabe, Osamu Yamada, Osamu Akita

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING   111 ( 4 )   408 - 413   2011.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SOC BIOSCIENCE BIOENGINEERING JAPAN  

    Aspergillus oryzae AB390, a derivative of A. oryzae OR101, was found to be suitable for soy sauce production, yielding a product light brown in color. Compared to the parent strain, hemicellulase and cellulase activities in the mutant were higher; however, its amylase activity was found to be much lower. To determine the cause of these differences, the enzymatic profile change, as a function of the carbon source in submerged cultures, was examined. Amylase activity in AB390 was hardly detectable and not affected by the carbon source utilized. In the absence of starch where glucose could not be generated, hemicellulase and cellulase activities in both the parent and mutant were the same. A nonsense mutation was found in the upstream region of the putative transactivation domain of the transcriptional activator of the amylolytic genes, amyR in AB390. Complementation of AB390 with the wild-type amyR reduced hemicellulase and cellulase activities and increased amylase activity in soy sauce koji, the mold responsible for giving soy sauce. Northern analysis and two-dimensional (2-D) electrophoresis indicated that the unique enzymatic profile of AB390 was regulated transcriptionally. The results suggested that the loss of amyR function indirectly affected the production of hemicellulolytic and cellulolytic enzymes, likely through a carbon catabolite repression-mediated control. (C) 2010, The Society for Biotechnology, Japan. All rights reserved.

    DOI: 10.1016/j.jbiosc.2010.12.006

    Web of Science

    PubMed

    researchmap

  • Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering Reviewed

    Yuichiro Kezuka, Masaki Kojima, Ryoji Mizuno, Kazushi Suzuki, Takeshi Watanabe, Takamasa Nonaka

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   78 ( 10 )   2295 - 2305   2010.8

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:WILEY-LISS  

    The rice class I chitinase OsChia1b, also referred to as RCC2 or Cht-2, is composed of an N-terminal chitin-binding domain (ChBD) and a C-terminal catalytic domain (CatD), which are connected by a proline- and threonine-rich linker peptide. Because of the ability to inhibit fungal growth, the OsChia1b gene has been used to produce transgenic plants with enhanced disease resistance. As an initial step toward elucidating the mechanism of hydrolytic action and antifungal activity, the full-length structure of OsChia1b was analyzed by X-ray crystallography and small-angle X-ray scattering (SAXS). We determined the crystal structure of full-length OsChia1b at 2.00-angstrom resolution, but there are two possibilities for a biological molecule with and without interdomain contacts. The SAXS data showed an extended structure of OsChia1b in solution compared to that in the crystal form. This extension could be caused by the conformational flexibility of the linker. A docking simulation of ChBD with tri-N-acetylchitotriose exhibited a similar binding mode to the one observed in the crystal structure of a two-domain plant lectin complexed with a chitoo-ligosaccharide. A hypothetical model based on the binding mode suggested that ChBD is unsuitable for binding to crystalline alpha-chitin, which is a major component of fungal cell walls because of its collisions with the chitin chains on the flat surface of alpha-chitin. This model also indicates the difference in the binding specificity of plant and bacterial ChBDs of GH19 chitinases, which contribute to antifungal activity. Proteins 2010; 78:2295-2305. (C) 2010 Wiley-Liss, Inc.

    DOI: 10.1002/prot.22742

    Web of Science

    PubMed

    researchmap

  • Improved Transformation of the Halo-Tolerant Yeast Zygosaccharomyces rouxii by Electroporation Reviewed

    Jun Watanabe, Kenji Uehara, Yoshinobu Mogi, Kazushi Suzuki, Takeshi Watanabe, Tatsuo Yamazaki

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   74 ( 5 )   1092 - 1094   2010.5

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    To improve the transformation efficiency of Zygosaccharomyces rouxii by electroporation, glycerol was added to the electroporation buffer and the cells were frozen at -80 degrees C. These alterations drastically increased transformation efficiency, and we found that competent cells can be preserved at -80 degrees C without decreasing their transformation efficiency for at least 30d.

    DOI: 10.1271/bbb.90865

    Web of Science

    PubMed

    researchmap

  • Functional analysis of loop structures in the catalytic domain of rice class I chitinase

    S. OKADA, S. SUGIYAMA, R. MIZUNO, T. FUKAMIZO, Y. NISHIZAWA, Y. KEZUKA, T. NONAKA, K. SUZUKI, T.WATANABE

    Proceedings The 11th International Conference on Chitin and Chitosan & The 8th Asia-Pacific Chitin and Chitosan Symposium   10140   2009.9

     More details

    Language:English  

    researchmap

  • Role of three aromatic residues in the chitin binding domain Chi18aC from Streptomyces coelicolor A3(2)

    M. UEMURA, N. YAMADA, K. AKAGI, S. YOSHIO, T. IKEGAMI, K. SUZUKI, T.WATANABE

    Proceedings The 11th International Conference on Chitin and Chitosan & The 8th Asia-Pacific Chitin and Chitosan Symposium   10143   2009.9

     More details

    Language:English  

    researchmap

  • Local structure feature of the catalytic domain of rice class I chitinase

    S. SUGIYAMA, S. OKADA, R. MIZUNO, T. FUKAMIZO, Y. NISHIZAWA, Y. KEZUKA, T. NONAKA, K. SUZUKI, T.WATANABE

    Proceedings The 11th International Conference on Chitin and Chitosan & The 8th Asia-Pacific Chitin and Chitosan Symposium   10141   2009.9

     More details

    Language:English  

    researchmap

  • The role of exposed tryptophan and tyrosine residues on the surface of chitinase B from Serratia marcescens 2170

    Akiko MUTO, Asako OHARA, Kaori AZUMA, Kazushi SUZUKI, Takeshi WATANABE

    Biotechnology of Lignocellulose Degradation, Biomass Utilizattion and Biorefinery   14 ( 2 )   167   2008.9

     More details

    Language:English  

    J-GLOBAL

    researchmap

  • The importance of chitobiase and N-acetylglucosamine (GlcNAc) uptake in N,N '-diacetylchitoblose [(GlcNAC)(2)] utilization by Serratia marcescens 2170 Reviewed

    Tadayuki Toratani, Toshihiro Shoji, Tomonori Ikehara, Kazushi Suzuki, Takeshi Watanabe

    MICROBIOLOGY-SGM   154 ( 5 )   1326 - 1332   2008.5

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SOC GENERAL MICROBIOLOGY  

    N,N'-diacetylchitobiose [(GlcNAC)(2)] is the main degradation product from chitin by the action of chitinases of Serratia marcescens 2170. Uptake of (GlcNAC)(2) via a (GlcNAC)(2)-specific enzyme II permease by this bacterium has been demonstrated previously. Here, we report the contribution of chitobiase and N-acetylglucosamine (GlcNAc) uptake to the utilization of (GlcNAC)(2). When S. marcescens 2170 was cultivated in a medium containing chitin, chitobiase activity was detected both inside and outside the cells; intracellular chitobiase was more abundant and suggested to be mainly located in the periplasm. Production of chitobiase was induced by GlcNAc and more effectively by (GlcNAC)(2). For induction of chitobiase, uptake of (GlcNAC)(2) was essential but ChiR, an essential regulator of chitinase induction, was not required. S. marcescens 2170 grew well on both GlcNAc and (GlcNAC)(2) but mutants defective in either chitobiase or NagE, the GlcNAc-specific enzyme II permease, showed reduced growth on (GlcNAc)(2). These results suggest that, in addition to uptake as (GlcNAC)(2), a proportion of the (GlcNAC)(2) is converted to GlcNAc by chitobiase, mainly in the periplasm, and incorporated into the cytoplasm by NagE. The mutant defective in chitobiase grew more slowly on (GlcNAC)(2) than on GlcNAc, indicating that (GlcNAC)(2) is less efficiently fermented by S. marcescens 2170 in the absence of chitobiase. Therefore, uptake as both (GlcNAc)(2) and GlcNAc is important for efficient utilization of (GlcNAC)(2) in S. marcescens.

    DOI: 10.1099/mic.0.2007/016246-0

    Web of Science

    PubMed

    researchmap

  • Role of the loop structure of the catalytic domain in rice class I chitinase Reviewed

    Ryoji Mizuno, Tamo Fukamizo, Shinichi Sugiyama, Yoko Nishizawa, Yuichiro Kezuka, Takamasa Nonaka, Kazushi Suzuki, Takeshi Watanabe

    JOURNAL OF BIOCHEMISTRY   143 ( 4 )   487 - 495   2008.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:OXFORD UNIV PRESS  

    In the three-dimensional structure of a rice class I chitinase (OsChia1b) determined recently, a loop structure (loop II) is located at the end of the substrate-binding cleft, and is thus suggested to be involved in substrate binding. In order to test this assumption, deletion of the loop II region from the catalytic domain of OsChia1b and replacement of Trp159 in loop II with Ala were carried out. The loop II deletion and the W159A mutation increased hydrolytic activity not only towards (GlcNAc)(6) but also towards polysaccharide substrates. Similar results were obtained for k(cat)/K-m values determined for substrate reduced-(GlcNAc)(5). The two mutations shifted the splitting positions in (GlcNAc)(6) to the reducing end side, but the shift was less intensive in the Trp mutant. Theoretical analysis of the reaction time course indicated that sugar residue affinity at the +3 subsite was reduced from -2kcal/mol to +0.5 kcal/mol by loop II deletion. Reduced affinity at the +3 subsite might enhance the release of product fragments, resulting in higher turnover and higher enzymatic activities. Thus, we concluded that loop II is involved in sugar residue binding at the +3 subsite, but that Trp159 itself appears to contribute only partly to sugar residue interaction at the subsite.

    DOI: 10.1093/jb/mvn004

    Web of Science

    PubMed

    researchmap

  • Purification and characterization of a rice class I chitinase, OsChia1b, produced in Esherichia coli Reviewed

    Ryoji Mizuno, Yoshikane Itoh, Yoko Nishizawa, Yuichiro Kezuka, Kazushi Suzuki, Takamasa Nonaka, Takeshi Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   72 ( 3 )   893 - 895   2008.3

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    To determine the properties and structure of OsChia1b, a family 19 chitinase from Oryza sativa L. cv. Nipponbare (japonica sp.), recombinant OsChia1b was produced in Esherichia coli cells and purified to homogeneity by chitin affinity column chromatography. OsChia1b was highly active against soluble chitinous substrate, but not against crystalline chitin, and clearly inhibited hyphal extension of Trichoderma reesei.

    DOI: 10.1271/bbb.706931

    Web of Science

    PubMed

    researchmap

  • Antifungal chitinases: structure, function and possible application to biocontrol

    T. WATANABE, R. MIZUNO, K. SUZUKI, Y. KEZUKA, T. NONAKA, Y. NISHIZAWA

    Proceeding of the 1st international meeting for development of IPM in Asia and Africa   88 - 94   2007.11

     More details

    Language:English  

    researchmap

  • pH-dependent activation of the BarA-UvrY two-component system in Escherichia coli Reviewed

    Veronica Mondragon, Bernardo Franco, Kristina Jonas, Kazushi Suzuki, Tony Romeo, Ojar Melefors, Dimitris Georgellis

    JOURNAL OF BACTERIOLOGY   188 ( 23 )   8303 - 8306   2006.12

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The barA and uvrY genes of Escherichia coli encode a two-component sensor kinase and a response regulator, respectively. Although this system plays a major role in the regulation of central carbon metabolism, motility, and biofilm formation by controlling the expression of the CsrB and CsrC noncoding RNAs, the environmental conditions and the physiological signal(s) to which it responds remain obscure. In this study, we explored the effect of external pH on the activity of BarA/UvrY. Our results indicate that a pH lower than 5.5 provides an environment that does not allow activation of the BarA/UvrY signaling pathway.

    DOI: 10.1128/JB.01052-06

    Web of Science

    PubMed

    researchmap

  • Comprehensive alanine-scanning mutagenesis of Escherichia coli CsrA defines two subdomains of critical functional importance Reviewed

    Jeffrey Mercante, Kazushi Suzuki, Xiaodong Cheng, Paul Babitzke, Tony Romeo

    JOURNAL OF BIOLOGICAL CHEMISTRY   281 ( 42 )   31832 - 31842   2006.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

    The RNA-binding protein CsrA (carbon storage regulator) of Escherichia coli is a global regulator of gene expression and is representative of the CsrA/RsmA family of bacterial proteins. These proteins act by regulating mRNA translation and stability and are antagonized by binding to small noncoding RNAs. Although the RNA target sequence and structure for CsrA binding have been well defined, little information exists concerning the protein requirements for RNA recognition. The three-dimensional structures of three CsrA/RsmA proteins were recently solved, revealing a novel protein fold consisting of two interdigitated monomers. Here, we performed comprehensive alanine- scanning mutagenesis on csrA of E. coli and tested the 58 resulting mutants for regulation of glycogen accumulation, motility, and biofilm formation. Quantitative effects of these mutations on expression of glgCA'-'lacZ, flhDC'-'lacZ, and pgaA'-'lacZ translational fusions were also examined, and eight of the mutant proteins were purified and tested for RNA binding. These studies identified two regions of the amino acid sequence that were critical for regulation and RNA binding, located within the first (beta(1), residues 2-7) and containing the last (beta(5), residues 40-47) beta-strands of CsrA. The beta(1) and beta(5) strands of opposite monomers lie adjacent and parallel to each other in the three-dimensional structure of this protein. Given the symmetry of the CsrA dimer, these findings imply that two distinct RNA binding surfaces or functional subdomains lie on opposite sides of the protein.

    DOI: 10.1074/jbc.M606057200

    Web of Science

    PubMed

    researchmap

  • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E Reviewed

    Kazushi Suzuki, Paul Babitzke, Sidney R. Kushner, Tony Romeo

    GENES & DEVELOPMENT   20 ( 18 )   2605 - 2617   2006.9

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT  

    In Escherichia coli, the global regulatory protein CsrA (carbon store regulator A) binds to leader segments of target mRNAs, affecting their translation and stability. CsrA activity is regulated by two noncoding RNAs, CsrB and CsrC, which act by sequestering multiple CsrA dimers. Here, we describe a protein (CsrD) that controls the degradation of CsrB/CRNAs. The dramatic stabilization of CsrB/C RNAs in a csrD mutant altered the expression of CsrA-controlled genes in a manner predicted from the previously described Csr regulatory circuitry. A deficiency in RNase E, the primary endonuclease involved in mRNA decay, also stabilized CsrB/C, although the half-lives of other RNAs that are substrates for RNase E (rpsO, rpsT, and RyhB) were unaffected by csrD. Analysis of the decay of CsrB RNA, both in vitro and in vivo, suggested that CsrD is not a ribonuclease. Interestingly, the CsrD protein contains GGDEF and EAL domains, yet unlike typical proteins in this large superfamily, its activity in the regulation of CsrB/C decay does not involve cyclic di-GMP metabolism. The two predicted membrane-spanning regions are dispensable for CsrD activity, while HAMP-like, GGDEF, and EAL domains are required. Thus, these studies demonstrate a novel process for the selective targeting of RNA molecules for degradation by RNase E and a novel function for a GGDEF-EAL protein.

    DOI: 10.1101/gad.1461606

    Web of Science

    PubMed

    researchmap

  • CsrA post-transcriptionally represses pgaABCD, responsible for synthesis of a biofilm polysaccharide adhesin of Escherichia coli Reviewed

    Wang, X, AK Dubey, K Suzuki, CS Baker, P Babitzke, T Romeo

    MOLECULAR MICROBIOLOGY   56 ( 6 )   1648 - 1663   2005.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:BLACKWELL PUBLISHING LTD  

    The RNA-binding protein CsrA represses biofilm formation, while the non-coding RNAs CsrB and CsrC activate this process by sequestering CsrA. We now provide evidence that the pgaABCD transcript, required for the synthesis of the polysaccharide adhesin PGA (poly-beta-1,6-N-acetyl-D-glucosamine) of Escherichia coli, is the key target of biofilm regulation by CsrA. csrA disruption causes an approximately threefold increase in PGA production and an approximately sevenfold increase in expression of a pgaA'-'lacZ translational fusion. A Delta csrB Delta csrC mutant exhibits a modest decrease in pgaA'-'lacZ expression, while the response regulator UvrY, a transcriptional activator of csrB and csrC, stimulates this expression. Biofilm formation is not regulated by csrA, csrB or uvrY in a Delta pgaC mutant, which cannot synthesize PGA. Gel mobility shift and toeprint analyses demonstrate that CsrA binds cooperatively to pgaA mRNA and competes with 30S ribosome subunit for binding. CsrA destabilizes the pgaA transcript in vivo. RNA footprinting and boundary analyses identify six apparent CsrA binding sites in the pgaA mRNA leader, the most extensive arrangement of such sites in any mRNA examined to date. Substitution mutations in CsrA binding sites overlapping the Shine - Dalgarno sequence and initiation codon partially relieve repression by CsrA. These studies define the crucial mechanisms, though not the only means, by which the Csr system influences biofilm formation.

    DOI: 10.1111/j.1365-2958.2005.04648.x

    Web of Science

    PubMed

    researchmap

  • CsrA regulates translation of the Escherichia coli carbon starvation gene, cstA, by blocking ribosome access to the cstA transcript Reviewed

    AK Dubey, CS Baker, K Suzuki, AD Jones, P Pandit, T Romeo, P Babitzke

    JOURNAL OF BACTERIOLOGY   185 ( 15 )   4450 - 4460   2003.8

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    CsrA is a global regulator that binds to two sites in the glgCAP leader transcript, thereby blocking ribosome access to the glgC Shine-Dalgarno sequence. The upstream CsrA binding site (GCACACGGAU) was used to search the Escherichia colt genomic sequence for other genes that might be regulated by CsrA. cstA contained an exact match that overlapped its Shine-Dalgarno sequence. cstA was previously shown to be induced by carbon starvation and to encode a peptide transporter. Expression of a cstA'-'lacZ translational fusion in wild-type and csrA mutant strains was examined. Expression levels in the csrA mutant were approximately twofold higher when cells were grown in Luria broth (LB) and 5- to 10-fold higher when LB was supplemented with glucose. It was previously shown that cstA is regulated by the cyclic AMP (CAMP)-cAMP receptor protein complex and transcribed by Esigma(70). We investigated the influence of sigma(S) on cstA expression and found that a sigma(S) deficiency resulted in a threefold increase in cstA expression in wild-type and csrA mutant strains; however, CsrA-dependent regulation was retained. The mechanism of CsrA-mediated cstA regulation was also examined in vitro. Cross-linking studies demonstrated that CsrA is a homodimer. Gel mobility shift results showed that CsrA binds specifically to cstA RNA, while coupled-transcription-translation and toeprint studies demonstrated that CsrA regulates CstA synthesis by inhibiting ribosome binding to cstA transcripts. RNA footprint and boundary analyses revealed three or four CsrA binding sites, one of which overlaps the cstA Shine-Dalgarno sequence, as predicted. These results establish that CsrA regulates translation of cstA by sterically interfering with ribosome binding.

    DOI: 10.1128/JB.185.15.4450-4460.2003

    Web of Science

    PubMed

    researchmap

  • A novel sRNA component of the carbon storage regulatory system of Escherichia coli Reviewed

    T Weilbacher, K Suzuki, AK Dubey, Wang, X, S Gudapaty, Morozov, I, CS Baker, D Georgellis, P Babitzke, T Romeo

    MOLECULAR MICROBIOLOGY   48 ( 3 )   657 - 670   2003.5

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:WILEY-BLACKWELL  

    Small untranslated RNAs (sRNAs) perform a variety of important functions in bacteria. The 245 nucleotide sRNA of Escherichia coli , CsrC, was discovered using a genetic screen for factors that regulate glycogen biosynthesis. CsrC RNA binds multiple copies of CsrA, a protein that post-transcriptionally regulates central carbon flux, biofilm formation and motility in E. coli . CsrC antagonizes the regulatory effects of CsrA, presumably by sequestering this protein. The discovery of CsrC is intriguing, in that a similar sRNA, CsrB, performs essentially the same function. Both sRNAs possess similar imperfect repeat sequences (18 in CsrB, nine in CsrC), primarily localized in the loops of predicted hairpins, which may serve as CsrA binding elements. Transcription of csrC increases as the culture approaches the stationary phase of growth and is indirectly activated by CsrA via the response regulator UvrY. Because CsrB and CsrC antagonize CsrA activity and depend on CsrA for their synthesis, a csrB null mutation causes a modest compensatory increase in CsrC levels and vice versa. Homologues of csrC are apparent in several Enterobacteriaceae. The regulatory and evolutionary implications of these findings are discussed.

    DOI: 10.1046/j.1365-2958.2003.03459.x

    Web of Science

    researchmap

  • The Escherichia coli BarA-UvrY two-component system is needed for efficient switching between glycolytic and gluconeogenic carbon sources Reviewed

    AK Pernestig, D Georgellis, T Romeo, K Suzuki, H Tomenius, S Normark, O Melefors

    JOURNAL OF BACTERIOLOGY   185 ( 3 )   843 - 853   2003.2

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The Escherichia coli BarA and UvrY proteins were recently demonstrated to constitute a novel two-component system, although its function has remained largely elusive. Here we show that mutations in the sensor kinase gene, barA, or the response regulator gene, uvrY, in uropathogenic E. coli drastically affect survival in long-term competition cultures. Using media with gluconeogenic carbon sources, the mutants have a clear growth advantage when competing with the wild type, but using media with carbon sources feeding into the glycolysis leads to a clear growth advantage for the wild type. Results from competitions with mutants in the carbon storage regulation system, CsrA/B, known to be a master switch between glycolysis and gluconeogenesis, led us to propose that the BarA-UvrY two-component system controls the Csr system. Taking these results together, we propose the BarA-UvrY two-component system is crucial for efficient adaptation between different metabolic pathways, an essential function for adaptation to a new environment.

    DOI: 10.1128/JB.185.3.843-853.2003

    Web of Science

    PubMed

    researchmap

  • Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli Reviewed

    K Suzuki, Wang, X, T Weilbacher, AK Pernestig, O Melefors, D Georgellis, P Babitzke, T Romeo

    JOURNAL OF BACTERIOLOGY   184 ( 18 )   5130 - 5140   2002.9

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The global regulator CsrA (carbon storage regulator) is an RNA binding protein that coordinates central carbon metabolism, activates flagellum biosynthesis and motility, and represses biofilm formation in Escherichia coli. CsrA activity is antagonized by the untranslated RNA CsrB, to which it binds and forms a globular ribonucleoprotein complex. CsrA indirectly activates csrB transcription, in an apparent autoregulatory mechanism. In the present study, we elucidate the intermediate regulatory circuitry of this system. Mutations affecting the BarA/UvrY two-component signal transduction system decreased csrB transcription but did not affect csrA'-'lacZ expression. The uvrYdefect was severalfold more severe than that of barA. Both csrA and urrY were required for optimal barA expression. The latter observation suggests an autoregulatory loop for UvrY. Ectopic expression of uvrY suppressed the csrB-lacZ expression defects caused by uvrY, csrA, or barA mutations; csrA suppressed csrA or barA defects; and barA complemented only the barA mutation. Purified UvrY protein stimulated csrB-lacZ expression approximately sixfold in S-30 transcription-translation reactions, revealing a direct effect of UvrY on csrB transcription. Disruption of sdiA, which encodes a LuxR homologue, decreased the expression of uvrY'-'lacZ and csrB-lacZ fusions but did not affect csrA'-'lacZ. The BarA/UvrY system activated biofilm formation. Ectopic expression of uvrY stimulated biofilm formation by a csrB-null mutant, indicative of a CsrB-independent role for UvrY in biofilm development. Collectively, these results demonstrate that uvrY resides downstream from csrA in a signaling pathway for csrB and that CsrA stimulates UvrY-dependent activation of csrB expression by BarA-dependent and -independent mechanisms.

    DOI: 10.1128/JB.184.18.5130-5140.2002

    Web of Science

    PubMed

    researchmap

  • CsrA regulates glycogen biosynthesis by preventing translation of glgC in Escherichia coli Reviewed

    CS Baker, Morozov, I, K Suzuki, T Romeo, P Babitzke

    MOLECULAR MICROBIOLOGY   44 ( 6 )   1599 - 1610   2002.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:BLACKWELL PUBLISHING LTD  

    The carbon storage regulatory system of Escherichia coli controls the expression of genes involved in carbohydrate metabolism and cell motility. CsrA binding to glgCAP transcripts inhibits glycogen metabolism by promoting glgCAP mRNA decay. CsrB RNA functions as an antagonist of CsrA by sequestering this protein and preventing its action. In this paper, we elucidate further the mechanism of CsrA-mediated glgC regulation. Results from gel shift assays demonstrate that several molecules of CsrA can bind to each glgC transcript. RNA footprinting studies indicate that CsrA binds to the glgCAP leader transcript at two positions. One of these sites overlaps the glgC Shine-Dalgarno sequence, whereas the other CsrA target is located further upstream in an RNA hairpin. Results from toeprint and cell-free translation experiments indicate that bound CsrA prevents ribosome binding to the glgC Shine-Dalgarno sequence and that this reduces GlgC synthesis. The effect of two deletions in the upstream binding site was examined. Both of these deletions reduced, but did not eliminate, CsrA binding in vitro and CsrA-dependent regulation in vivo . Our findings establish that bound CsrA inhibits initiation of glgC translation, thereby reducing glycogen biosynthesis. This inhibition of translation probably contributes to destabilization of the glgC transcript that was observed previously.

    DOI: 10.1046/j.1365-2958.2002.02982.x

    Web of Science

    PubMed

    researchmap

  • Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: Enzymatic properties and synergism on chitin degradation Reviewed

    K Suzuki, N Sugawara, M Suzuki, T Uchiyama, F Katouno, N Nikaidou, T Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   66 ( 5 )   1075 - 1083   2002.5

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    To discover the individual roles of the chitinases from Serratia marcescens 2170, chitinases A, B, and C1 (ChiA, ChiB, and ChiC1) were produced by Escherichia coli and their enzymatic properties as well as synergistic effect on chitin degradation were studied. All three chitinases showed a broad pH optimum and maintained significant chitinolytic activity between pH 4 and 10. ChiA was the most active enzyme toward insoluble chitins, but ChiC1 was the most active toward soluble chitin derivatives among the three chitinases. Although all three chitinases released (GlcNAO(2) almost exclusively from colloidal chitin, ChiB and ChiC1 split (GlcNAc)(6) to (GlcNAc)(3), while ChiA exclusively generated (GlcNAc)(2) and (GlcNAc)(4). Clear synergism on the hydrolysis of powdered chitin was observed in the combination between ChiA and either ChiB or ChiC, and the sites attacked by ChiA on the substrate are suggested to be different from those by either ChiB or ChiC1.

    DOI: 10.1271/bbb.66.1075

    Web of Science

    researchmap

  • Biofilm formation and dispersal under the influence of the global regulator CsrA of Escherichia coli Reviewed

    DW Jackson, K Suzuki, L Oakford, JW Simecka, ME Hart, T Romeo

    JOURNAL OF BACTERIOLOGY   184 ( 1 )   290 - 301   2002.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The predominant mode of growth of bacteria in the environment is within sessile, matrix-enclosed communities known as biofilms. Biofilms often complicate chronic and difficult-to-treat infections by protecting bacteria from the immune system, decreasing antibiotic efficacy, and dispersing planktonic cells to distant body sites. While the biology of bacterial biofilms has become a major focus of microbial research, the regulatory mechanisms of biofilm development remain poorly defined and those of dispersal are unknown. Here we establish that the RNA binding global regulatory protein CsrA (carbon storage regulator) of Escherichia coli K-12 serves as both a repressor of biofilm formation and an activator of biofilm dispersal under a variety of culture conditions. Ectopic expression of the E. coli K-12 csrA gene repressed biofilm formation by related bacterial pathogens. A csrA knockout mutation enhanced biofilm formation in E. coli strains that were defective for extracellular, surface, or regulatory factors previously implicated in biofilm formation. In contrast, this csrA mutation did not affect biofilm formation by a glgA (glycogen synthase) knockout mutant. Complementation studies with gig genes provided further genetic evidence that the effects of CsrA on biofilm formation are mediated largely through the regulation of intracellular glycogen biosynthesis and catabolism. Finally, the expression of a chromosomally encoded csrA'-'lacZ translational fusion was dynamically regulated during biofilm formation in a pattern consistent with its role as a repressor. We propose that global regulation of central carbon flux by CsrA is an extremely important feature of E. coli biofilm development.

    DOI: 10.1128/JB.184.1.290-301.2002

    Web of Science

    PubMed

    researchmap

  • Regulatory interactions of Csr components: the RNA binding protein CsrA activates csrB transcription in Escherichia coli Reviewed

    S Gudapaty, K Suzuki, Wang, X, P Babitzke, T Romeo

    JOURNAL OF BACTERIOLOGY   183 ( 20 )   6017 - 6027   2001.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The global regulator CsrA (carbon storage regulator) of Escherichia coli is a small RNA binding protein that represses various metabolic pathways and processes that are induced in the stationary phase of growth, while it activates certain exponential phase functions. Both repression and activation by CsrA involve posttranscriptional mechanisms, in which CsrA binding to mRNA leads to decreased or increased transcript stability, respectively. CsrA also binds to a small untranslated RNA, CsrB, forming a ribonucleoprotein complex, which antagonizes CsrA activity. We have further examined the regulatory interactions of CsrA and CsrB RNA. The 5' end of the CsrB transcript was mapped, and a csrB::cam null mutant was constructed. CsrA protein and CsrB RNA levels were estimated throughout the growth curves of wild-type and isogenic csrA, csrB, rpoS, or csrA rpoS mutant strains. CsrA levels exhibited modest or negligible effects of these mutations. The intracellular concentration of CsrA exceeded the total CsrA-binding capacity of intracellular CsrB RNA. In contrast, CsrB levels were drastically decreased (similar to 10-fold) in the csrA mutants. CsrB transcript stability was unaffected by csrA. The expression of a csrB-lacZ transcriptional fusion containing the region from -242 to +4 bp of the csrB gene was decreased similar to 20-fold by a csrA::kanR mutation in vivo but was unaffected by CsrA protein in vitro. These results reveal a significant, though most likely indirect, role for CsrA in regulating csrB transcription. Furthermore, our findings suggest that CsrA mediates an intriguing form of autoregulation, whereby its activity, but not its levels, is modulated through effects on an RNA antagonist, CsrB.

    DOI: 10.1128/JB.183.20.6017-6027.2001

    Web of Science

    researchmap

  • LysR-type transcriptional regulator ChiR is essential for production of all chitinases and a chitin-binding protein, CBP21, in Serratia marcescens 2170 Reviewed

    K Suzuki, T Uchiyama, M Suzuki, N Nikaidou, M Regue, T Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   65 ( 2 )   338 - 347   2001.2

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    To identify the genes required for chitinase production by Serratia marcescens 2170, various Tn5 mutants somehow defective in chitinase production were isolated in a previous study. In order to identify the mutated gene in one of the chitinase-deficient mutants, N1, DNA regions flanking the Tn5 insertion were cloned and sequenced. Sequence comparison showed that the mutation occurred in the ORF located between chiB and cbp, which encode chitinase B and chitin-binding protein CBP21, respectively. The ORF encodes a 313-amino acid polypeptide which has significant similarity with various LysR-type transcriptional regulators, and thus the gene was designated chiR. Targeted mutagenesis confirmed that disruption of the chiR gene results in the phenotype of N1. Gel mobility shift assays using partially purified ChiR protein demonstrated that this protein specifically binds to the intergenic region between chiR and cbp. These results strongly suggest that ChiR is a LysR-type transcriptional regulator which is essential for production of all chitinases and CBP21.

    DOI: 10.1271/bbb.65.338

    Web of Science

    researchmap

  • Chitinase system and chitinase deficient mutants of Serratia marcescens 2170.

    Suzuki, K, T. Uchiyama, M. Suzuki, M. Taiyoji, N. Nikaidou, T. Watanabe

    Genetics, Biochemistry and Ecology of Cellulose Degradation.   673 - 682   1999.12

     More details

    Language:English   Publishing type:Research paper (international conference proceedings)  

    researchmap

  • The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases Reviewed

    K Suzuki, M Taiyoji, N Sugawara, N Nikaidou, B Henrissat, T Watanabe

    BIOCHEMICAL JOURNAL   343 ( 3 )   587 - 596   1999.11

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:PORTLAND PRESS  

    The third chitinase gene (chiC) of Serratia marcescens 2170, specifying chitinases C1 and C2, was identified. Chitinase C1 lacks a signal sequence and consists of a catalytic domain belonging to glycoside hydrolase family 18, a fibronectin type III-like domain (Fn3 domain) and a C-terminal chitin-binding domain (ChBD). Chitinase C2 corresponds to the catalytic domain of C1 and is probably generated by proteolytic removal of the Fn3 and ChBDs. The loss of the C-terminal portion reduced the hydrolytic activity towards powdered chitin and regenerated chitin, but not towards colloidal chitin and glycol chitin, illustrating the importance of the ChBD for the efficient hydrolysis of crystalline chitin. Phylogenetic analysis showed that bacterial family 18 chitinases can be clustered in three subfamilies which have diverged at an early stage of bacterial chitinase evolution. Ser. marcescens chitinase C1 is found in one subfamily, whereas chitinases A and B of the same bacterium belong to another subfamily. Chitinase C1 is the only Ser. marcescens chitinase that has an Fn3 domain. The presence of multiple, divergent, chitinases in a single chitinolytic bacterium is perhaps necessary for efficient synergistic degradation of chitin.

    DOI: 10.1042/0264-6021:3430587

    Web of Science

    researchmap

  • Prodigiosin produced by Serratia marcescens enhances the insecticidal activity of Bacillus thuringiensis delta-endotoxin (Cry1C) against common cutworm, Spodoptera litura Reviewed

    S Asano, K Ogiwara, Y Nakagawa, K Suzuki, H Hori, T Watanabe

    JOURNAL OF PESTICIDE SCIENCE   24 ( 4 )   381 - 385   1999

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:PESTICIDE SCI SOC JAPAN  

    Synergistic effects of chitinases A, B and C1, chitin binding protein and prodigiosin from Serratia marcescens on the insecticidal activity of delta-endotoxin, CrylC, of Bacillus thuringiensis against the common cutworm, Spodoptera litura, were investigated. Only prodigiosin showed a potent synergistic activity with CrylC on both the lethal and growth inhibitory activity. In the previous paper (Asano et al., 1999) a synergistic effect in the supernatants of S. marcescens culture on the insecticidal activity of CrylC was described. The supernatants from S. marcescens and partially purified prodigiosin showed a similar synergistic activity on the insecticidal activity of CrylC. The content of prodigiosin in the supernatants was estimated as 10% according to the absorbance at 467 nm where prodigiosin showed a peak and the content seemed to be enough to explain the synergistic activity of the supernatants on the activity of CrylC.

    DOI: 10.1584/jpestics.24.381

    Web of Science

    Scopus

    researchmap

  • Synergistic effects of supernatants from Serratia marcescens culture on larvicidal activity of Bacillus thuringiensis Cry1C toxin against common cutworm, Spodoptera litura Reviewed

    S Asano, K Suzuki, H Hori, T Watanabe

    JOURNAL OF PESTICIDE SCIENCE   24 ( 1 )   44 - 48   1999

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:PESTICIDE SCI SOC JAPAN  

    The supernatants of Serratia marcescens culture was shown to possess an enhancing effect on the larvicidal activity of Bacillus thuringiensis delta-endotoxin (Cry1C) against the common cutworm, Spodoptera litura. The synergistic effect was observed in both larval mortality and growth inhibition. The synergistic activity increased in proportion to the increment either of the supernatant or Cry1C concentration. The addition of supernatants of S. marcescens culture to Cry1C was able to enhance the insecticidal activity of delta-endotoxin over 8 fold compared with that of toxin alone. The synergism was very high to the insecticidal activity against S, litura but not in other three lepidopterous insects tested, i.e., Mamestra brassicae, Plutella xylostella and Adoxophyes honmai. Therefore the synergistic activity of the supernatants of S, marcescens culture seemed to be specific to insect species.

    DOI: 10.1584/jpestics.24.44

    Web of Science

    researchmap

  • Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170 Reviewed

    K Suzuki, M Suzuki, M Taiyoji, N Nikaidou, T Watanabe

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   62 ( 1 )   128 - 135   1998.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    A chitin binding protein (CBP21) 21kDa in size, is a major protein in the culture snpernatant when Serratia marcescens 2170 is grown in the presence of chitin, The gene (cbp) for CBP21 was found to be located in a region 1.5 kb downstream of the chiB gene encoding chitinase B. The cbp gene encodes a polypeptide of 197 amino-acids with a calculated size of 21.6 kDa containing a putative signal sequence of 27 amino acids. Comparison of the amino acid sequence of the deduced polypeptide with that of other proteins showed that CBP21 is similar (45.3% amino acid identity) to CHB1 of Streptomyces olivaceoviridis. Purified CBP21 prepared from the periplasmic fraction of Escherichia coli carrying the cloned cbp gene showed its highest binding activity to squid chitin (beta-chitin) followed by colloidal chitin and regenerated chitin. Binding of CBP21 to regenerated chitin was affected by pH, in particular, low pH reduced binding activity markedly. The presence of similar chitin binding proteins in the distantly related microorganisms, Streptomyces and Serratia, suggests a wide distribution of this type of chitin binding protein in chitinolytic microorganisms.

    DOI: 10.1271/bbb.62.128

    Web of Science

    researchmap

  • Genetic analysis of the chitinase system of Serratia marcescens 2170 Reviewed

    T Watanabe, K Kimura, T Sumiya, N Nikaidou, K Suzuki, M Suzuki, M Taiyoji, S Ferrer, M Regue

    JOURNAL OF BACTERIOLOGY   179 ( 22 )   7111 - 7117   1997.11

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    To carry out a genetic analysis of the degradation and utilization of chitin by Serratia marcescens 2170, various Tn5 insertion mutants with characteristic defects in chitinase production were isolated and partially characterized. Prior to the isolation of the mutants, proteins secreted into culture medium in the presence of chitin were analyzed. Four chitinases, A, B, C1, and C2, among other proteins, were detected in the culture supernatant of S. marcescens 2170. All four chitinases and a 21-kDa protein (CBP21) lacking chitinase activity shelved chitin binding activity. Cloning and sequencing analysis of the genes encoding Chitinases A and B of strain 2170 revealed extensive similarities to those of other strains of S. marcescens described previously. Tn5 insertion mutagenesis of strain 2170 was carried out, and mutants which formed altered clearing zones of colloidal chitin were selected. The obtained mutants were divided into five classes as follows: mutants with (i) no clearing zones, (ii) fuzzy clearing zones, (iii) large clearing zones, (iv) delayed clearing zones, and (v) small clearing zones. Preliminary characterization suggested that some of these mutants have defects in chitinase excretion, a negatively regulating mechanism of chitinase gene expression, an essential factor for chitinase gene expression, and a structural gene for a particular chitinase. These mutants could allow researchers to identify the genes involved in the degradation and utilization of chitin by S. marcescens 2170.

    Web of Science

    researchmap

  • PURIFICATION AND SOME PROPERTIES OF CHITINASE-B1 FROM BACILLUS-CIRCULANS WL-12 Reviewed

    T WATANABE, T YAMADA, W OYANAGI, K SUZUKI, H TANAKA

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   56 ( 4 )   682 - 683   1992.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    DOI: 10.1271/bbb.56.682

    Web of Science

    researchmap

  • STRUCTURE OF THE GENE ENCODING CHITINASE-D OF BACILLUS-CIRCULANS WL-12 AND POSSIBLE HOMOLOGY OF THE ENZYME TO OTHER PROKARYOTIC CHITINASES AND CLASS-III PLANT CHITINASES Reviewed

    T WATANABE, W OYANAGI, K SUZUKI, K OHNISHI, H TANAKA

    JOURNAL OF BACTERIOLOGY   174 ( 2 )   408 - 414   1992.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    The gene (chiD) encoding the precursor of chitinase D was found to be located immediately upstream of the chiA gene, encoding chitinase A1, which is a key enzyme in the chitinase system of Bacillus circulans WL-12. Sequencing analysis revealed that the deduced polypeptide encoded by the chiD gene was 488 amino acids long and the distance between the coding regions of the chiA and chiD genes was 103 bp. Remarkable similarity was observed between the N-terminal one-third of chitinase D and the C-terminal one-third of chitinase A1. The N-terminal 47-amino-acid segment (named ND) of chitinase D showed a 61.7% amino acid match with the C-terminal segment (CA) of chitinase A1. The following 95-amino-acid segment (R-D) of chitinase D showed 62.8 and 60.6% amino acid matches, respectively, to the previously reported type III-like repeating units R-1 and R-2 in chitinase A1, which were shown to be homologous to the fibronectin type III sequence. A 73-amino-acid segment (residues 247 to 319) located in the putative activity domain of chitinase D was found to show considerable sequence similarity not only to other bacterial chitinases and class III higher-plant chitinases but also to Streptomyces plicatus endo-beta-N-acetylglucosaminidase H and the Kluyveromyces lactis killer toxin alpha-subunit. The evolutionary and functional meanings of these similarities are discussed.

    Web of Science

    researchmap

  • GENE CLONING OF CHITINASE-A1 FROM BACILLUS-CIRCULANS WL-12 REVEALED ITS EVOLUTIONARY RELATIONSHIP TO SERRATIA CHITINASE AND TO THE TYPE-III HOMOLOGY UNITS OF FIBRONECTIN Reviewed

    T WATANABE, K SUZUKI, W OYANAGI, K OHNISHI, H TANAKA

    JOURNAL OF BIOLOGICAL CHEMISTRY   265 ( 26 )   15659 - 15665   1990.9

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

    Web of Science

    researchmap

  • CHITINASE SYSTEM OF BACILLUS-CIRCULANS WL-12 AND IMPORTANCE OF CHITINASE-A1 IN CHITIN DEGRADATION Reviewed

    T WATANABE, W OYANAGI, K SUZUKI, H TANAKA

    JOURNAL OF BACTERIOLOGY   172 ( 7 )   4017 - 4022   1990.7

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC MICROBIOLOGY  

    Web of Science

    researchmap

  • Expression in escherichia coli of the bacillus circulans wl-12 structural gene for β-1, 3-glucanase a Reviewed

    Takeshi Watanabe, Naokazu Yahata, Yasushi Nakamura, Yoshimitsu Muramoto, Kazushi Suzuki, Shusei Kamimiya, Hirosato Tanaka, Takeshi Watanabe

    Agricultural and Biological Chemistry   53 ( 7 )   1759 - 1767   1989

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Bacillus circulans WL-12, a yeast and fungal cell wall lytic bacterium, secretes a variety of polysaccharide degrading enzymes into the culture medium. When β-l, 3-glucanase was induced with pachyman, a β-1, 3-glucose polymer obtained from the tree fungus Poria cocus Wolf, six distinct active molecules of the enzyme with different molecular weights were detected in the culture supernatant of this bacterium. Molecular cloning of one of the β-l, 3-glucanase genes into E. coli was achieved by transforming E. coli HB101 cells with recombinant plasmids composed of chromosomal DNA fragments prepared from B. circulans WL-12 and the plasmid vector pUC 19. A recombinant plasmid containing 4.4 kb of inserted DNA in the Pst I site of pUC 19, designated as pNT003, conferred the ability to degrade pachyman on E. coli cells. The presence of pNT003 was harmful for E. coli cells and caused cell lysis, especially at higher temperatures of cultivation. β-l, 3-Glucanase activity detected in E. coli was mainly recovered in the periplasmic fraction when cell lysis did not occur. SDS-PAGE analysis revealed that the periplasmic fraction contained four active molecules of β-l, 3-glucanase which corresponded to four of the six active molecules produced by B. circulans WL-12. © 1989 Agricultural Chemical Society of Japan.

    DOI: 10.1080/00021369.1989.10869584

    Scopus

    researchmap

▶ display all

MISC

  • 転写因子ChiRによるSerratia plymuthicaのキチン分解酵素系制御

    高橋柚衣, 石田知輝, PENTEKHINA Iuliia, PENTEKHINA Iuliia, 樋口響, 田中麻祐希, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    キチン・キトサン研究(Web)   30 ( 1 )   2024

  • Kinetic analysis of processive degradation reactions by two chitinases, BcChiA1 and SmChiA.

    豊泉伶奈, 小出優衣, 中澤颯, 鈴木一史, 鈴木一史, 杉本華幸, 杉本華幸

    日本農芸化学会大会講演要旨集(Web)   2023   2023

  • Regulation of PNAG biosynthesis and biofilm formation by the Csr system in Escherichia coli

    鈴木一史, 鈴木一史, 石黒志実, 岡村龍盛, 小谷果穂, 竹内真美, 杉本華幸, 杉本華幸

    キチン・キトサン研究(Web)   29 ( 2 )   2023

  • Regulation of the chitinolytic enzyme system by the transcription factor ChiR in Serratia plymuthica

    高橋柚衣, 石田知輝, PENTEKHINA Iuliia, PENTEKHINA Iuliia, 樋口響, 田中麻祐希, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    キチン・キトサン研究(Web)   29 ( 2 )   2023

  • ′′Sakeology′′ Started at Niigata University

    鈴木一史, 岸保行, 平田大

    日本醸造協会誌   118 ( 2 )   80 - 86   2023

  • The effect of RNA chaperone Hfq on chitinase system of Serratia plymuthica

    石田知輝, 小嶋優常, 樋口響, 高橋柚衣, LIOU Shih-Ting, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2023   2023

  • 総合大学の強みを生かした新潟大学における「日本酒学」の取り組み

    鈴木 一史

    産学官連携ジャーナル   18 ( 8 )   8 - 10   2022

     More details

    Language:Japanese   Publisher:国立研究開発法人 科学技術振興機構  

    ※本記事に抄録はありません。

    DOI: 10.1241/sangakukanjournal.18.8_8

    researchmap

  • 文理融合・組織連携 総合大学の強みを生かした新潟大学における「日本酒学」の取り組み

    鈴木一史

    産学官連携ジャーナル(Web)   18 ( 8 )   2022

  • Serratia plymuthicaにおけるsRNAを介したキチン分解利用系の制御

    石田知輝, 小嶋優常, 樋口響, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 鈴木一史

    キチン・キトサン研究(Web)   28 ( 1 )   2022

  • Unfolding mechanism and stability of a chitin-active lytic polysaccharide monooxygenase, CBP21

    小島佳織, 中島優一, 鈴木一史, 鈴木一史, 杉本華幸

    キチン・キトサン研究(Web)   28 ( 2 )   2022

  • Chitinolytic enzyme system of Serratia plymuthica and the regulatory mechanism of its expression

    鈴木一史, 鈴木一史, 鈴木一史, PENTEKHINA Iuliia, PENTEKHINA Iuliia, 石田知輝, 樋口響, 杉本華幸, 杉本華幸

    キチン・キトサン研究(Web)   28 ( 2 )   2022

  • Regulation of Chitinase System by small RNA ChiX and Hfq in Serratia plymuthica

    樋口響, 石田知輝, 小嶋優常, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2022   2022

  • Structural stability of FnIII domains of bacterial glycoside hydrolases

    太田垣太朗, 鈴木一史, 鈴木一史, 杉本華幸

    日本農芸化学会大会講演要旨集(Web)   2022   2022

  • Analysis of CsrD amino acid residues in control of Csr sRNA decay

    吉田将来, GLADYSHCHUK Olga, 藤樫紅梅, 岡村龍盛, 小谷果穂, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2022   2022

  • Analysis of CsrD, a stability regulator of small RNAs in Csr system

    吉田将来, 山田竣太, 石黒志実, 岡村龍盛, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2021   2021

  • Regulation of chitin-degrading enzyme system by small RNA in Serratia plymuthica

    小嶋優常, 堀井恭子, 宗像直輝, 熊木智耶, 石田知輝, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2021   2021

  • Regulation of Chitinase System by sRNA in Serratia plymuthica

    石田知輝, 小嶋優常, 樋口響, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 鈴木一史

    キチン・キトサン研究(Web)   27 ( 2 )   2021

  • 多糖モノオキシゲナーゼCBP21の変性反応-銅イオンの効果-

    中島優一, 鈴木一史, 杉本華幸

    日本蛋白質科学会年会プログラム・要旨集   21st   2021

  • Isolation and breeding of sake yeast from wisteria flower in Niigata

    鈴木聖袈, 鈴木雅史, 栗林喬, 佐藤圭吾, 武内沙樹, 菖池陽平, 杉本華幸, 杉本華幸, 金桶光起, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2020   2020

  • 新潟県内の清酒製造場における「蔵付き酵母」の分離とその醸造特性

    栗林喬, 畠山明, 浅野宏文, 古田悟, 原崇, 鈴木一史, 城斗志夫, 金桶光起, 小熊哲哉, 渡邉剛志, 渡邉剛志

    日本醸造協会誌   115 ( 11 )   2020

  • 新潟県内の清酒製造場における「蔵付き酵母」の分離とその醸造特性

    栗林喬, 畠山明, 浅野宏文, 古田悟, 原崇, 鈴木一史, 城斗志夫, 金桶光起, 小熊哲哉, 渡邉剛志, 渡邉剛志

    日本醸造学会大会講演要旨集(CD-ROM)   2020   2020

  • Unfolding mechanism and structural stability of a lytic polysaccharide monooxygenase, CBP21

    杉本華幸, 杉本華幸, 中村禄朗, 中島優一, 坪田侑里香, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2020   2020

  • Regulation of chitinase system by small RNA ChiX and Hfq in Serratia

    小嶋優常, 宗像直輝, 熊木智耶, 堀井恭子, 山岸拓矢, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2020   2020

  • 大腸菌におけるCsr小分子RNAの安定性制御因子CsrDの解析

    山田竣太, 吉田将来, 石黒志実, 杉本華幸, 鈴木一史

    日本分子生物学会年会プログラム・要旨集(Web)   43rd   2020

  • Bacillus circulans由来連続分解型キチナーゼの-3サブサイトの解析

    多田瑞季, 渡邉美咲, 鈴木一史, 鈴木一史, 杉本華幸, 杉本華幸

    日本細胞生物学会大会(Web)   71st   2019

  • 細菌におけるsmall RNA ChiXによるmRNAの再標的化機構の解析

    小嶋優常, 宗像直輝, 堀井恭子, 山岸拓矢, 熊木智耶, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本RNA学会年会要旨集   21st   2019

  • ジスルフィド結合がキチン分解モノオキシゲナーゼCBP21の構造安定性に及ぼす影響について

    中村禄朗, 中島優一, 鈴木一史, 鈴木一史, 渡邊剛志, 渡邊剛志, 杉本華幸, 杉本華幸

    日本細胞生物学会大会(Web)   71st   2019

  • 大腸菌におけるCsrDによるsmall RNA CsrBの分解制御とCsrシステムの利用

    山田竣太, 石黒志実, 坂井航, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2019   2019

  • 多糖モノオキシゲナーゼ,CBP21の構造安定性-金属イオンの効果-

    杉本華幸, 杉本華幸, 中島優一, 中村禄朗, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2019   2019

  • EIIA<sup>Glc</sup>およびCsrDによる大腸菌のsmall RNA CsrB安定性制御機構の解析

    山田竣太, 石黒志実, 井上智恵, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本分子生物学会年会プログラム・要旨集(Web)   42nd   2019

  • Analysis of Chitin degradation enzymes from Aeromonas salmonicida

    服部達之, TRAN Dinh Minh, TRAN Dinh Minh, PENTEKHINA Iuliia, PENTEKHINA Iuliia, 渡邉剛志, 杉本華幸, 鈴木一史

    キチン・キトサン研究   25 ( 2 )   2019

  • 大腸菌におけるsmall RNA CsrB安定性制御とCsrシステムを利用したpoly-β-1,6-GlcNAc産生

    石黒志実, 山田竣太, 坂井航, 井上智恵, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本RNA学会年会要旨集   21st   2019

  • 大腸菌における小分子RNA CsrBの半減期にあたえるCsrDと炭素源の濃度による影響

    山田竣太, 天木拓海, 杉本華幸, 鈴木一史

    日本RNA学会年会要旨集   20th   2018

  • 小分子RNA ChiXを介した2種のmRNAの転写後調節

    山岸拓矢, 堀井恭子, 宗像直輝, 南晴香, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2018   2018

  • 連続反応性をもつ3種のキチナーゼによる基質分解反応の速度論的解析

    多田瑞季, 小田陽介, 猪浦弾, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志, 杉本華幸, 杉本華幸

    日本蛋白質科学会年会プログラム・要旨集   18th   2018

  • 小分子RNA ChiXによる2種の標的mRNAの翻訳制御

    宗像直輝, 堀井恭子, 山岸拓矢, 小嶋優常, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本RNA学会年会要旨集   20th   2018

  • 多糖モノオキシゲナーゼ,CBP21の構造安定性

    杉本華幸, 本山彩香, 片桐絵里奈, 渡邉剛志, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2018   2018

  • 大腸菌における小分子RNA CsrBの半減期にあたえるCsrDと炭素源の影響

    天木拓海, 山田竣太, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本RNA学会年会要旨集   19th   2017

  • 細菌の小分子RNAによるキチン分解系とキチン分解産物取り込み系の制御機構

    堀井恭子, 南晴香, 山岸拓矢, 宗像直輝, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    キチン・キトサン研究   23 ( 2 )   2017

  • 2種のターゲットmRNAによる小分子RNA ChiXの制御

    堀井恭子, 宗像直輝, 山岸拓矢, 南晴香, 杉本華幸, 渡邉剛志, 鈴木一史, 杉本華幸, 渡邉剛志, 鈴木一史

    日本RNA学会年会要旨集   19th   2017

  • 大腸菌Csrシステムにおける小分子RNA CsrBの分解制御

    天木拓海, 坂井航, 山田竣太, 飯田和奏, 渡邉剛志, 渡邉剛志, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史

    日本微生物生態学会大会(Web)   2017   2017

  • 大腸菌における小分子RNA CsrBの分解制御機構

    鈴木一史, 鈴木一史, 天木拓海, 坂井航, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本ゲノム微生物学会年会要旨集   11th   2017

  • 大腸菌CsrDによる小分子RNA CsrBの分解制御

    天木拓海, 坂井航, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2017   2017

  • Serratia marcescensキチナーゼBの結晶性キチン分解機構の解明-触媒クレフト入口の芳香族アミノ酸残基の役割について-

    杉本華幸, 杉本華幸, 出澤有太, 猪浦弾, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2016   2016

  • Serratia marcescens2170の多糖モノオキシゲナーゼCBP21欠損株の性質

    桜井大地, 小柳くるみ, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   22 ( 2 )   2016

  • Serratia marcescens2170の多糖モノオキシゲナーゼCBP21の生理機能の解明

    桜井大地, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2016   2016

  • 小分子RNA・ChiXによるchiR発現抑制とその解除

    鈴木一史, 鈴木一史, 南晴香, 山岸拓矢, 小川知佐奈, 佐々木直美, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2016   2016

  • Small RNA ChiXによる2種の標的mRNAの発現制御機構

    南晴香, 鈴木一史, 鈴木一史, 佐々木直美, 山岸拓矢, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本ゲノム微生物学会年会要旨集   10th   2016

  • Effects of the tryptophan residue at the subsite-3 on the processive hydrolysis mechanism of Serratia marcescens chitinase A

    杉本華幸, 杉本華幸, 猪浦弾, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   22 ( 2 )   2016

  • Studies on the ligand binding mechanism of the chitin binding domain of chitinase 18aC from Streptomyces coelicolor

    杉本華幸, 杉本華幸, 小林豊, 鈴木一史, 鈴木一史, 池上貴久, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   21 ( 2 )   130 - 131   2015.7

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • Mechanism of crystalline chitin hydrolysis by a unique enzyme, Serratia marcescens chitinase B

    藤沼晶子, 丸屋良輔, 杉本華幸, 杉本華幸, 中村啓太, 橋詰義夫, 五十嵐圭日子, 鮫島正浩, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   15th ( 2 )   2015

  • Analysis of the genes encoding poly-β-1,6-GlcNAc biosynthetic and degrading enzymes in bacteria

    鈴木一史, 鈴木一史, 天木拓海, 南晴香, 茶原麻衣, 宮崎裕介, 坂井航, 大辻大貴, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   21 ( 2 )   2015

  • 大腸菌におけるGGDEF/EALドメインタンパク質YliE/YliFの機能解析

    草間慶弘, 渡部大樹, 今野環, 久下貴紀, 塚田海斗, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2015   2015

  • Serratia marcescens2170のキチン分解利用機構の解析:ChiD,Ctbの発現系構築とCBP21欠損株の構築

    今井裕也, 五十嵐瑞礎, 三浦拓馬, 桜井大地, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2015   2015

  • 大腸菌CsrシステムにおけるCsrB RNAの分解過程の解析

    阿部葉月, 天木拓海, 伊藤学, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本ゲノム微生物学会年会要旨集   9th   2015

  • Serratia marcescensにおける小分子RNA ChiXを介したchiR及びchiPQ-ctbの発現制御

    鈴木一史, 鈴木一史, 南晴香, 小川知佐奈, 佐々木直美, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本RNA学会年会要旨集   17th   2015

  • Special feature Invited Reviewed

    Sugimoto Hayuki, Igarashi Kiyohiko, Uchihashi Takayuki, Suzuki Kazushi, Watanabe Takeshi

    Bulletin of Applied Glycoscience   4 ( 2 )   107 - 112   2014.5

     More details

    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:The Japanese Society of Applied Glycoscience  

    DOI: 10.5458/bag.4.2_107

    CiNii Article

    CiNii Books

    J-GLOBAL

    researchmap

  • Chitin degradation and utilization system of Serratia marcescens 2170-Functional analysis of the chiPQ-ctb operon- Invited Reviewed

    三浦拓馬, 本間祥太, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   20 ( 1 )   4 - 15   2014.4

     More details

    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    J-GLOBAL

    researchmap

  • Serratia marcescens2170由来CBP21のファミリー19キチナーゼによるキチン分解への効果

    高橋亮大, 森山拓実, 猪又義広, 杉本華幸, 中川裕子, 鈴木一史, 戸谷一英, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2014   2D02P16 (WEB ONLY)   2014.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • Small RNA ChiXが制御するSerratia marcescensキチン分解利用系の解析

    鈴木一史, 鈴木一史, 南晴香, 小川知佐奈, 佐々木直美, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本RNA学会年会要旨集   16th   2014

  • 大腸菌CsrシステムにおけるCsrB RNA分解過程の解析

    伊藤学, 岡山明裕, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本RNA学会年会要旨集   16th   2014

  • small RNAを介したSerratia marcescensキチン分解利用系制御へのNagC及びChbRの関与

    鈴木一史, 鈴木一史, 小川知佐奈, 南晴香, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2014   2014

  • Serratia marcescens2170のキチン分解利用機構-chiPQ-ctbオペロンの機能-

    三浦拓馬, 今井裕也, 小川知佐奈, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2014   2014

  • 大腸菌におけるCsrB RNAの分解過程の解析

    伊藤学, 岡山明裕, 阿部葉月, 高橋優介, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2014   2014

  • Bacterial chitinases ad chitin degradation and utulization system

    渡邉剛志, 杉本華幸, 鈴木一史

    キチン・キトサン研究   20 ( 2 )   2014

  • 構造一体型キチナーゼSerratia marcescensキチナーゼBの結晶性キチン分解機構の解明とフレキシブル型キチナーゼとの比較解析

    杉本華幸, 杉本華幸, 中村啓太, 西野裕史, 藤沼晶子, 橋詰義夫, 丸屋良輔, 五十嵐圭日子, 鮫島正浩, 渡辺大輝, 内橋貴之, 安藤敏夫, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2013   2013

  • Serratia marcescensのCsrシステム及びCsrB/C RNAの安定性を制御するCsrDの機能解析

    伊藤学, 野村和希, 高橋優介, 杉本華幸, 渡邉剛志, 鈴木一史, 杉本華幸, 渡邉剛志, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2013   2013

  • 大腸菌におけるCsrB RNA分解産物の解析

    伊藤学, 岡山明裕, 高橋優介, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本分子生物学会年会プログラム・要旨集(Web)   36th   2013

  • 転写調節因子ChiRを介したMicM sRNAによるSerratia marcescensキチナーゼ遺伝子群発現制御

    鈴木一史, 鈴木一史, 小川知佐奈, 佐々木直美, 高野慎也, 清水麻里, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2013   2013

  • Regulation of chitinase gene expression by incorporation of chitin degradation products and small RNA in Serratia marcescens

    SUZUKI Kazushi, SASAKI Naomi, OGAWA Chisana, TAKANO Shinya, SUGIMOTO Hayuki, WATANABE Takeshi

    キチン・キトサン研究   18 ( 2 )   132 - 133   2012.7

     More details

  • Serratia marcescensキチナーゼBの結晶性キチン分解機構の解明

    杉本華幸, 杉本華幸, 藤沼晶子, 中村啓太, 西野裕史, 五十嵐圭日子, 鮫島正浩, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • 高速原子間力顕微鏡観察を用いたSerratia marcescensキチナーゼBの結晶性キチン分解機構の解明

    杉本華幸, 杉本華幸, 藤沼晶子, 中村啓太, 西野裕史, 五十嵐圭日子, 鮫島正浩, 渡辺大輝, 内橋貴之, 安藤敏夫, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本生化学会大会(Web)   85th   2012

  • 大腸菌におけるGGDEF-EALドメインタンパク質CsrDによるsmall RNA半減期の調節

    高橋優介, 岡山明裕, 伊藤学, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2012   2012

  • Serratia marcescensキチン分解利用関連遺伝子の破壊と機能解析

    本間祥太, 三浦拓馬, 高野慎也, 佐々木直美, 小川知佐奈, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • モジュール型キチナーゼによる結晶性キチン分解機構の解析

    橋詰義夫, 丸屋良輔, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • Streptomyces griseus由来推定キチン結合タンパクの異種発現と機能解析

    工藤まどか, 中川裕子, 鈴木一史, 渡邉剛志, 戸谷一英

    日本農芸化学会大会講演要旨集(Web)   2012   2012

  • Serratia marcescens CsrDによるsmall RNAの安定性制御

    伊藤学, 野村和希, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • small RNAによるSerratia marcescensキチン分解利用遺伝子群の発現制御

    鈴木一史, 鈴木一史, 佐々木直美, 小川知佐奈, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • 異なるファミリーに属するキチナーゼによる各種キチンの分解特性

    高橋亮大, 竹本由衣, 大塚未来, 中川裕子, 戸谷一英, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会関東支部講演要旨集   2012 ( Oct )   2012

  • Serratia marcescensキチン分解利用関連遺伝子の遺伝子破壊

    高野慎也, 佐々木直美, 本間祥太, 小川知佐奈, 杉本華幸, 杉本華幸, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集(Web)   2012   2012

  • MicM sRNAによるSerratia marcescensキチン分解利用系の制御

    鈴木一史, 鈴木一史, 清水麻里, 佐々木直美, 小川知佐奈, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志

    日本分子生物学会年会プログラム・要旨集(Web)   35th   2012

  • 大腸菌におけるGGDEF/EALドメインタンパク質の機能解析

    塚田海斗, 渡部大樹, 杉本華幸, 杉本華幸, 渡邉剛志, 渡邉剛志, 鈴木一史, 鈴木一史

    日本農芸化学会大会講演要旨集(Web)   2012   2012

  • Degradation characteristics of the chitinases with different tertiary structures on the various types of chitin

    TAKEMOTO Yui, OTSUKA Miku, NAKAGAWA Yuko, TOTANI Kazuhide, SUZUKI Kazushi, WATANABE Takeshi

    キチン・キトサン研究   17 ( 2 )   194 - 195   2011.7

     More details

  • キチン結合ドメインの立体構造と結合特性の比較解析

    植村迪夫, 大塚未来, 丸屋良輔, 奥村明子, 池上貴久, 苅田修一, 毛塚雄一郎, 野中孝昌, 杉本華幸, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   17 ( 2 )   234 - 234   2011.7

     More details

  • キチン結合ドメインの結合特性の比較解析

    植村迪夫, 丸屋良輔, 遠藤陽太, 苅田修一, 蟹江美佐, 池上貴久, 奥村明子, 毛塚雄一郎, 野中孝昌, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2011   203   2011.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • 各種キチナーゼによるメカノケミカル粉砕キチンの分解特性

    竹本由衣, 大塚未来, 中川裕子, 戸谷一英, 鈴木一史, 鈴木一史, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集   2011   2011

  • カイコにおける昆虫サイトカインによる自然免疫制御機構の解明

    石井健一, 浜本洋, 神村学, 鈴木一史, 渡邉剛志, 今村亮俊, 安達健朗, 関水和久

    生化学   2011

  • Regulation of chitinase gene expression by small RNA in Serratia marcescens

    鈴木一史, 鈴木一史, 清水麻里, 佐々木直美, 渡邉剛志, 渡邉剛志

    キチン・キトサン研究   17 ( 2 )   208 - 209   2011

     More details

  • Serratia marcescensにおけるsmall RNAによるキチナーゼ発現の制御

    鈴木一史, 鈴木一史, 清水麻里, 佐々木直美, 虎谷忠幸, 渡邉剛志, 渡邉剛志

    日本農芸化学会大会講演要旨集   2011   2011

  • Regulation of chitinase system by small RNA in Serratia marcescens

    SUZUKI Kazushi, SHIMIZU Mari, TAKANO Shinya, TORATANI Tadayuki, WATANABE Takeshi

    16 ( 2 )   170 - 171   2010.6

     More details

  • 細菌キチナーゼキチン結合ドメインの結合特性の比較解析

    植村迪夫, 丸屋良輔, 山田伸明, 原政司, 池上貴久, 毛塚雄一郎, 野中孝昌, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2010   160   2010.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • Crystalline chitin hydrolysis by chitinases from Serratia marcescens

    渡邉剛志, 渡邉剛志, 武藤亜紀子, 工藤江利子, 鈴木一史, 鈴木一史, 五十嵐圭日子, 鮫島正浩

    キチン・キトサン研究   16 ( 2 )   128 - 129   2010

     More details

  • 大腸菌CsrB RNAの分解機構

    鈴木一史, 伊藤学, 岡山明裕, 水野孝彦, 渡邉剛志, ROMEO Tony

    日本農芸化学会大会講演要旨集   2010   2010

  • Construction of CBP21 knock-out mutant of Serratia marcescens 2170 and its properties

    KAWAMI Hisako, USUI KIMIHITO, SUZUKI Kazushi, MUTOH Akiko, SEKIMIZU Kzuhisa, WATANABE Takeshi

    16 ( 2 )   202   2010

     More details

  • 大腸菌におけるCsrB RNA分解中間産物の解析

    鈴木一史, 鈴木一史, 岡山明裕, 伊藤学, 渡邉剛志, 渡邉剛志, ROMEO Tony

    日本RNA学会年会要旨集   12th   2010

  • Serratia marcescens 2170のCBP21欠損株の構築と性質の解析

    川見寿子, 臼井公人, 鈴木一史, 武藤亜紀子, 関水和久, 渡邉剛志

    日本農芸化学会大会講演要旨集   2010   2010

  • セラチア菌のO抗原によるカイコ血球細胞の細胞死誘導

    石井健一, 臼井公人, 今村亮俊, 浜本洋, 鈴木一史, 渡邉剛志, 関水和久

    生化学   2010

  • 土壌放線菌由来キチン分解酵素Chi18aCの基質吸着ドメインのNMRによる立体構造の解析

    奥村明子, 近石絵理子, 高井朋代, 吉尾幸子, 森田潤司, 植村迪夫, 鈴木一史, 渡邉剛志, 池上貴久

    生化学   82回   ROMBUNNO.2P-230 - 230   2009.9

     More details

    Language:Japanese   Publisher:(公社)日本生化学会  

    J-GLOBAL

    researchmap

  • Streptomyces griseus HUT6037由来キチナーゼCの構造と機能の解明

    吉田優, 川見寿子, 菅丈司, 水野亮二, 毛塚雄一郎, 野中孝昌, 池上貴久, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2009   47   2009.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • イネクラスIキチナーゼ活性ドメインにおけるループ構造の機能解析

    杉山真一, 水野亮二, 岡田真司, 西澤洋子, 深溝慶, 毛塚雄一郎, 野中孝昌, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2009   2009

  • Local structural feature of the catalytic domains of family 19 chitinases and hydrolysis products from chitin

    杉山真一, 岡田真司, 深溝慶, 毛塚雄一郎, 野中孝昌, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   15 ( 2 )   160 - 161   2009

     More details

  • Lactobacillus sakei KLB 3138aC株の特性と清酒醸造への応用

    木村貴一, 大野剛, 木村(新野)葉子, 高橋慶太郎, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2009   2009

  • Structural and functional analysis of chitinase C from Streptomyces griseus HUT6037

    吉田優, 水野亮二, 菅丈司, 毛塚雄一郎, 野中孝昌, 池上貴久, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   14 ( 2 )   238 - 238   2008.7

     More details

  • Streptomyces griseus HUT6037由来キチナーゼCの構造と機能の解明

    吉田優, 菅丈司, 水野亮二, 毛塚雄一郎, 野中孝昌, 池上貴久, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2008   34   2008.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • イネクラスIキチナーゼ活性ドメインのループIIの機能解析

    杉山真一, 水野亮二, 西澤洋子, FUKAMIZO Tamo, 毛塚雄一郎, 野中孝昌, 鈴木一史, 渡邉剛志

    生化学   2008

  • The importance of ybfM 5’-UTR for chitinase expression in Serratia marcescens 2170

    虎谷忠幸, 山内友恵, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   14 ( 2 )   237   2008

     More details

  • 大腸菌CsrB/C RNAの安定性を制御するCsrDの解析

    水野孝彦, 渡邉剛志, ROMEO Tony, 鈴木一史

    生化学   2008

  • 転写因子chiRを破壊したSerratia marcescensのプロテオーム解析

    庄司俊裕, 虎谷忠幸, 宮本勝城, 辻坊裕, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2008   2008

  • 大腸菌small RNA CsrB/Cの安定性を制御するCsrDのアラニン置換変異による解析

    藤生康宏, 水野孝彦, ROMEO Tony, 渡邉剛志, 鈴木一史

    日本農芸化学会大会講演要旨集   2008   2008

  • The role of exposed tryptophan and tyrosine residues in chitinase B from Serratia marcescens 2170

    MUTO Akiko, OHARA Asako, AZUMA Kaori, SUZUKI Kazushi, WATANABE Takeshi

    2008 ( 2 )   236   2008

     More details

  • Serratia marcescensのキチナーゼ発現におけるybfM5′-UTRの重要性

    虎谷忠幸, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2008   2008

  • Streptomyces griseus HUT6037キチナーゼCのキチン吸着機構

    菅丈司, 山田伸明, 水野亮二, 野中孝昌, 毛塚雄一郎, 池上貴久, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2007   62   2007.3

     More details

    Language:Japanese  

    J-GLOBAL

    researchmap

  • Post-transcriptional regulation by the Csr global regulatory system in Escherichia coli.

    Suzuki, K

    Bull. Facul. Agric. Niigata Univ.   59 ( 2 )   56 - 63   2007.3

     More details

    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:Niigata University  

    In many species of bacteria, the Csr (carbon storage regulator) global regulatory system coordinates the expression of various genes. In Escherichia coli, the central component of this system, CsrA, is a RNA-binding protein. The CsrA is a homodimer and binds to leader segments of target mRNAs, affecting their translation and stability. CsrA activity is regulated by two small non-coding RNAs, CsrB and CsrC. These RNAs contain multiple CsrA-binding sequences and act by sequestering CsrA. In this system, CsrA indirectly activates transcription of csrB and csrC through a two-component signal transduction system, BarA/UvrY. Another component of this system, CsrD, controls the degradation of CsrB and CsrC RNAs. CsrD contains GGDEF and EAL signaling domains, however, unlike typical GGDEF and EAL domain proteins, its activity does not involve cyclic di-GMP metabolism. The dramatic stabilization of CsrB and CsrC RNAs in a csrD mutant altered the expression of CsrA-regulated genes. The Csr components, CsrA, CsrB and CsrC RNAs, and CsrD, interact within the autoregulatory circuit that provides a homeostatic mechanism for control of CsrA activity.

    CiNii Article

    CiNii Books

    researchmap

    Other Link: http://www.agr.niigata-u.ac.jp/study_report/report/59-02/056-063.pdf

  • The GGDEF-EAL protein, CsrD, regulates the decay of the small RNAs CsrB and CsrC.

    Kazushi Suzuki

    25 ( 3 )   397 - 401   2007.2

     More details

    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    researchmap

  • Functional analysis of family 19 chitinase from Vibrio fischeri MKT20

    水野亮二, 大橋大輔, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   13 ( 2 )   210   2007

     More details

  • Characterization of an operon involved in chitin utilization by Serratia marcescens 2170

    虎谷忠幸, 庄司俊裕, 鈴木一史, 渡邉剛志

    キチン・キトサン研究   13 ( 2 )   160 - 161   2007

     More details

  • Serratia marcescens 2170のキチナーゼの発現に関与する外膜蛋白質

    虎谷忠幸, 鈴木一史, 渡邉剛志

    日本農芸化学会大会講演要旨集   2007   2007

  • Regulatory interactions of Csr components: the RNA binding protein CsrA activates csrB transcription in Escherichia coli (vol 183, pg 6017, 2001)

    S Gudapaty, K Suzuki, Wang, X, P Babitzke, T Romeo

    JOURNAL OF BACTERIOLOGY   184 ( 3 )   871 - 871   2002.2

     More details

    Language:English   Publisher:AMER SOC MICROBIOLOGY  

    Web of Science

    researchmap

  • BT剤のハスモンヨトウ殺虫活性を増進させるSerratia marcescensの産生物質

    浅野昌司, 荻原克俊, 鈴木一史, 渡辺剛志, 仲川洋二, 堀秀隆

    蚕糸・昆虫農業技術研究所研究資料   ( 27 )   2000

  • chitinase system of Serratia marcescens 2170

    UCHIYAMA Taku, SUZUKI Kazusi, YAMAGUCHI Jyunko, KANEKO Ryousuke, NIKAIDOU Naoki, WATANABE Takeshi

    6 ( 2 )   154 - 155   2000

     More details

  • Recognition of LacNAc-Oxazoline Derivative by Chitinase.

    正田晋一郎, CHAKAPAN L, 三沢義知, 渡辺剛志, 鈴木一史, 橋本昌征

    キチン・キトサン研究   5 ( 2 )   226 - 227   1999

     More details

  • A specific synergistic substance in supernatants of Serratia marcescens to Cry1C of Bacillus thuringiensis against the common cutworm, Spodoptera litura

    ASANO Shoji, OGIWARA Katsutoshi, SUZUKI Kazushi, WATANABE Takeshi, NAKAGAWA Yoji, HORI Hidetaka

    24th   82   1999

     More details

    Language:Japanese   Publisher:Pesticide Science Society of Japan  

    CiNii Article

    CiNii Books

    J-GLOBAL

    researchmap

  • Genetic Analysis of Chitinase System of Serratia marcescens 2170

    SUZUKI K., UCHIYAMA T., SUZUKI M., NIKAIDOU N., WATANABE T.

    4 ( 2 )   200 - 201   1998.5

     More details

  • Specific synergistic activity in supernatants of Serratia marcescens to Cry1C of Bacillus thuringiensis the common cutworm, Spodoptera litura

    ASANO Shoji, SUZUKI Kazushi, HORI Hidetaka, WATANABE Takeshi

    23rd   53   1998

     More details

    Language:Japanese   Publisher:Pesticide Science Society of Japan  

    CiNii Article

    CiNii Books

    J-GLOBAL

    researchmap

  • Molecular Characterization of Chitinases and Chitin Binding Protein from Serratia marcescens 2170

    SUZUKI K., TAIYOJI M., SUZUKI M, NIKAIDOU N., WATANABE T.

    キチン・キトサン研究   3 ( 2 )   180 - 181   1997.5

     More details

▶ display all

Awards

  • 長瀬研究振興賞

    2018.4   公益財団法人 長瀬科学技術振興財団   細菌におけるsmall RNAの安定性制御機構の解明とその応用

    鈴木 一史

     More details

Research Projects

  • Regulation of small RNA stability and gene expression in bacteria

    Grant number:22K05378

    2022.4 - 2025.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

      More details

    Grant amount:\4160000 ( Direct Cost: \3200000 、 Indirect Cost:\960000 )

    researchmap

  • Research on switching of mRNAs targeted by sRNA and regulation of sRNA stability in bacteria

    Grant number:19K05787

    2019.4 - 2022.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    SUZUKI Kazushi

      More details

    Grant amount:\4290000 ( Direct Cost: \3300000 、 Indirect Cost:\990000 )

    In bacteria, the antisense sRNA ChiX, which regulates the expression of the chitinase genes, switched the target mRNA from one to the other. In this process, base pairing between the terminator region of the sRNA and the mRNA was important. In the bacterial Csr system, the critical amino acid residue of CsrD that regulates the stability of protein-bound sRNA was identified. In addition, the activity of CsrD responded quickly to the external environment. The possibility of using this mechanism to produce polysaccharides, a component of bacterial biofilms, was demonstrated.

    researchmap

  • 細菌におけるsmall RNAの安定性制御機構の解明とその応用

    2018.4 - 2019.3

    System name:研究助成

    Awarding organization:公益財団法人 長瀬科学技術振興財団

    鈴木 一史

      More details

    Authorship:Principal investigator  Grant type:Competitive

    researchmap

  • Coordinated regulation of the expression network of genes encoding chitin-degradation and utilization system by small RNA

    Grant number:16K07659

    2016.4 - 2019.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    SUZUKI Kazushi, WATANABE takeshi

      More details

    Authorship:Principal investigator  Grant type:Competitive

    ChiX is a small RNA that coordinately regulates the gene expression of chitin-degrading enzymes and the uptake system of chitin degradation products in Serratia marcescens. Although ChiX suppressed the expression of chitin-degrading enzyme genes by suppressing its translation by base pairing with chiR mRNA encoding transcriptional factor, the expression of chiP led to the derepression of chiR by ChiX. The chiP mRNA was capable of base pairing with the region extending before and after the terminator of ChiX, which suggested that ChiX switched the target from chiR mRNA to chiP mRNA.

    researchmap

  • Elucidation of the mechanism underlying processive hydrolysis of crystalline chitin by bacterial chitinases.

    Grant number:15K07355

    2015.4 - 2018.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    Watanabe Takeshi, IGARASHI Kiyohiko, SUZUKI Kazushi, SUGIMOTO Hayuki

      More details

    Grant amount:\4940000 ( Direct Cost: \3800000 、 Indirect Cost:\1140000 )

    The ultimate goal of this research is proposition of the universal and evolved model of the mechanism for crystalline chitin degradation and utilization by chitinolytic bacteria. Therefore, "the role of the protein (CBP21) that promote degradation of crystalline chitin", "the importance of CBP21 for the biological and ecological function of the chitinolytic bacteria", "the mechanism for biodegradation of α-chitin that exists in nature more abundantly" were studied. As a results, it became clear that CBP21 is especially important for degradation and utilization of chitin close to natural condition, an amino acid residue with aromatic ring of big resonating structure at the entrance of the catalytic cleft of chitinase is very important for hydrolysis of highly crystalline chitin substrate, and that one chitinase molecule jump to another chitin chain in different orientation and begins hydrolysis in opposite direction.

    researchmap

  • Coordinated regulation of the chitin-degradation and utilization system by small RNA in bacteria

    Grant number:25450097

    2013.4 - 2016.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    Suzuki Kazushi, WATANABE Takeshi, MIYAMOTO Katushiro

      More details

    Authorship:Principal investigator  Grant type:Competitive

    Small RNA ChiX was expressed constitutively and repressed the translational initiation of chiR mRNA, encoding the transcriptional factor for the expression of chitin-degrading enzymes, by base paring in Serratia marcescens. When the chiPQ-ctb operon, encoding chitoporin and chitobiase, was fully expressed by degradation products of chitin, ChiX bound to the chiP mRNA. Base pairing between ChiX and the chiP mRNA relieved repression on the translational initiation of the chiR mRNA. Thus, the expressed ChiR activated the production of chitin-degrading enzymes. ChiX coordinates the synchronized expression of chitin-degrading enzymes and the system for incorporating chitin degradation products.

    researchmap

  • Elucidation of the role of aromatic amino acid residues in crystalline chitin hydrolysis and development to the mechanism of a-chitin hydrolysis

    Grant number:24580104

    2012.4 - 2015.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    WATANABE TAKESHI, IGARASHI Kiyohiko, SUZUKI Kazushi, SUGIMOTO Hayuki

      More details

    Grant amount:\5460000 ( Direct Cost: \4200000 、 Indirect Cost:\1260000 )

    Chitin is a crystalline and rigid structural polysaccharide present in a variety of organisms. Elucidation of the mechanism underlying in the enzymatic degradation of crystalline chitin is very important not only from enzymological and biological view points, but also for utilization of biomass resources. In this study, critical roles of the aromatic amino acid residues, which are present on the surface of chitinase molecule and inside of its catalytic cleft, in processive hydrolysis of crystalline chitin was demonstrated.

    researchmap

  • Functional analysis of GGDEF/EAL proteins that control the stability of small RNA

    Grant number:21580088

    2009.4 - 2012.3

    System name:Grants-in-Aid for Scientific Research

    Research category:Grant-in-Aid for Scientific Research (C)

    Awarding organization:Japan Society for the Promotion of Science

    SUZUKI Kazushi, TONY Romeo

      More details

    Authorship:Principal investigator  Grant type:Competitive

    To elucidate the mechanism of bacterial biofilm formation control, we analyzed the function of the GGDEF/EAL proteins in bacteria. GGDEF/EAL protein CsrD was not involved in c-di-GMP metabolism and altered the activity in each growth phase and controlled biofilm formation by regulating the stability of small RNA. On the other hand, YliF(GGDEF protein) and YliE(EAL protein) controlled biofilm formation by regulating the synthesis and degradation of c-di-GMP.

    researchmap

  • GGDEF/EAL蛋白質によるバイオフィルム制御機構

    2007.4 - 2009.3

    System name:科学研究費助成事業

    Research category:若手研究(スタートアップ)

    鈴木一史

      More details

    Authorship:Principal investigator  Grant type:Competitive

    自然環境中の固体表面に細菌が付着し形成する「バイオフィルム」の形成制御メカニズムを解明するため、small RNAの安定性を制御するGGDEF/EAL蛋白質CsrDと細胞内のシグナル物質c-di-GMPの代謝に関わるGGDEF/EAL蛋白質に関する研究を行った。CsrDの機能に重要と思われるアミノ酸残基をアラニン残基に置換した変異型CsrDの解析の結果、CsrDの活性に重要な領域が明らかとなった。また、GGDEF/EAL蛋白質は多糖であるPGAの産生を調節することでバイオフィルムを制御していることが明らかとなった。

    researchmap

▶ display all

 

Teaching Experience

  • 日本酒学概論I(自然科学)

    2022
    Institution name:新潟大学

  • 日本酒学A

    2022
    Institution name:新潟大学

  • 課題発掘・解決セミナーI

    2022
    Institution name:新潟大学

  • 農学入門II

    2022
    Institution name:新潟大学

  • 農学入門I

    2022
    Institution name:新潟大学

  • 醸造学

    2021
    -
    2023
    Institution name:新潟大学

  • 応用生命・食品科学概論

    2021
    Institution name:新潟大学

  • スタディ・スキルズAIc

    2021
    Institution name:新潟大学

  • スタディ・スキルズAIIc

    2021
    Institution name:新潟大学

  • 応用生命・食品科学セミナーIV

    2021
    Institution name:新潟大学

  • Topics in Molecular Microbiology

    2021
    Institution name:新潟大学

  • 食品科学概論

    2020
    -
    2021
    Institution name:新潟大学

  • 農学入門Ⅱ

    2019
    -
    2020
    Institution name:新潟大学

  • 農学入門Ⅰ

    2019
    -
    2020
    Institution name:新潟大学

  • 微生物学

    2018
    Institution name:新潟大学

  • 生命を知る

    2018
    Institution name:新潟大学

  • 日本酒学B

    2018
    -
    2022
    Institution name:新潟大学

  • 日本酒学A-2

    2018
    -
    2021
    Institution name:新潟大学

  • 日本酒学A-1

    2018
    -
    2021
    Institution name:新潟大学

  • 応用生物化学セミナーⅠ

    2018
    Institution name:新潟大学

  • 基礎化学

    2017
    Institution name:新潟大学

  • 分子微生物学

    2017
    Institution name:新潟大学

  • 応用生物化学科インターンシップ

    2016
    -
    2017
    Institution name:新潟大学

  • 科学英語演習

    2016
    -
    2017
    Institution name:新潟大学

  • 醸造学

    2015
    -
    2023
    Institution name:新潟大学

  • 自然科学総論Ⅳ

    2015
    Institution name:新潟大学

  • Topics in Molecular Microbiology

    2013
    -
    2021
    Institution name:新潟大学

  • 研究発表演習(中間発表)

    2012
    -
    2015
    Institution name:新潟大学

  • 文献詳読Ⅰ

    2012
    -
    2015
    Institution name:新潟大学

  • 生命・食料科学特定研究BⅡ

    2012
    -
    2015
    Institution name:新潟大学

  • 文献詳読Ⅱ

    2012
    -
    2015
    Institution name:新潟大学

  • 生命・食料科学特定研究BⅠ

    2012
    -
    2015
    Institution name:新潟大学

  • 生命・食料科学セミナーBⅡ

    2012
    -
    2015
    Institution name:新潟大学

  • 生命・食料科学セミナーBⅠ

    2012
    -
    2015
    Institution name:新潟大学

  • 応用生命・食品科学演習(学会発表)

    2012
    -
    2014
    Institution name:新潟大学

  • 分子生命科学演習Ⅰ

    2011
    -
    2019
    Institution name:新潟大学

  • 分子生命科学演習Ⅱ

    2011
    -
    2018
    Institution name:新潟大学

  • 応用生物化学概論

    2011
    -
    2017
    Institution name:新潟大学

  • 微生物化学特論

    2011
    -
    2013
    Institution name:新潟大学

  • 分子生命科学実験

    2010
    -
    2018
    Institution name:新潟大学

  • 微生物分子遺伝学

    2008
    Institution name:新潟大学

  • 微生物遺伝子制御学

    2008
    -
    2011
    Institution name:新潟大学

  • 微生物学実験

    2007
    Institution name:新潟大学

  • 遺伝子工学

    2007
    -
    2016
    Institution name:新潟大学

  • くらしと微生物

    2007
    -
    2016
    Institution name:新潟大学

  • 応用微生物学

    2007
    -
    2016
    Institution name:新潟大学

  • 生物学

    2007
    -
    2015
    Institution name:新潟大学

  • 微生物ゲノム工学

    2007
    Institution name:新潟大学

  • 微生物遺伝子工学

    2007
    Institution name:新潟大学

▶ display all

 

Social Activities

  • 出前講義:新潟県立佐渡高等学校

    Role(s): Lecturer

    2019.8

     More details

  • 出前講義:青森県立八戸北高等学校

    Role(s): Lecturer

    2017.10

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立柏崎高等学校

    Role(s): Lecturer

    2017.7

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立三条高等学校

    Role(s): Lecturer

    2016.12

     More details

    Audience: High school students

    researchmap

  • 出前講義:福島県立会津高等学校

    Role(s): Lecturer

    2016.10

     More details

    Audience: High school students

    researchmap

  • 出前講義:静岡県立島田高校

    Role(s): Lecturer

    2016.9

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立新津高等学校

    Role(s): Lecturer

    2016.7

     More details

    Audience: High school students

    researchmap

  • 出前講義:富山県立高岡南高等学校

    Role(s): Lecturer

    2016.6

     More details

    Audience: High school students

    researchmap

  • 出前講義:静岡県立静岡東高等学校

    Role(s): Lecturer

    2015.9

     More details

    Audience: High school students

    researchmap

  • 出前講義:國學院大学栃木高等学校

    Role(s): Lecturer

    2015.7

     More details

    Audience: High school students

    researchmap

  • 出前講義:福島県立葵高等学校

    Role(s): Lecturer

    2015.6

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立新津高等学校

    Role(s): Lecturer

    2014.10

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立巻高等学校

    Role(s): Editer

    2014.9

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立糸魚川高等学校

    Role(s): Lecturer

    2014.8

     More details

    Audience: High school students

    researchmap

  • 出前講義:新潟県立長岡向陵高等学校

    Role(s): Lecturer

    2014.7

     More details

    Audience: High school students

    researchmap

  • 出前講義:福島県立葵高等学校

    Role(s): Lecturer

    2014.6

     More details

    Audience: High school students

    researchmap

  • 高大連携科学講座(新潟南高校SSH事業)

    Role(s): Lecturer

    2012.10

     More details

    Audience: High school students

    researchmap

  • 高大連携科学講座(新潟南高校SSH事業)

    Role(s): Lecturer

    2011.6

     More details

    Audience: High school students

    researchmap

  • 会津高等学校会津大学講座

    Role(s): Lecturer

    2010.10

     More details

    Audience: High school students

    researchmap

▶ display all