Faculty of Science Associate Professor
Graduate School of Science and Technology Life and Food Sciences Associate Professor
College of Creative Studies Creative Studies Course Associate Professor
Updated on 2024/09/20
博士(農学) ( 2003.3 東京大学 )
修士(農学) ( 1999.3 東京大学 )
学士(理学) ( 1997.3 学習院大学 )
翻訳
リボソーム
遺伝子発現
DNA
X線結晶構造解析
タンパク質
RNA
Life Science / Structural biochemistry
Life Science / Molecular biology
Niigata University Faculty of Science/Graduate School of Science and Technology Life and Food Sciences Associate Professor
2019.4
Niigata University Faculty of Science/Graduate School of Science and Technology Life and Food Sciences Assistant Professor
2009.4 - 2019.3
Niigata University Center for Transdisciplinary Research Assistant Professor
2008.1 - 2009.3
The University of Tokyo Graduate School of Frontier Sciences
2007.4 - 2007.12
The University of Tokyo Graduate School of Agricultural and Life Sciences
2003.4 - 2007.3
Niigata University Creative Studies Course, College of Creative Studies Associate Professor
2021.4
Niigata University Faculty of Science Associate Professor
2019.4
Niigata University Graduate School of Science and Technology Life and Food Sciences Associate Professor
2019.4
Niigata University Faculty of Science Assistant Professor
2009.4 - 2019.3
Niigata University Graduate School of Science and Technology Life and Food Sciences Assistant Professor
2009.4 - 2019.3
Niigata University Center for Transdisciplinary Research Assistant Professor
2008.1 - 2009.3
The University of Tokyo Graduate School of Agricultural and Life Sciences Applied Biological Chemistry
1999.4 - 2003.3
The University of Tokyo Graduate School of Agricultural and Life Sciences Biotechnology
1997.4 - 1999.3
Gakushuin University Faculty of Science Department of Chemistry
1993.4 - 1997.3
THE MOLECULAR BIOLOGY SOCIETY OF JAPAN
JAPANESE SOCIETY FOR BACTERIOLOGY
THE RNA SOCIETY OF JAPAN
The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation. Reviewed International journal
Lei Yang, Ka-Ming Lee, Conny Wing-Heng Yu, Hirotatsu Imai, Andrew Kwok-Ho Choi, David K Banfield, Kosuke Ito, Toshio Uchiumi, Kam-Bo Wong
Nucleic acids research 50 ( 9 ) 5335 - 5348 2022.5
A novel ribosome-dimerization protein found in the hyperthermophilic archaeon Pyrococcus furiosus using ribosome-associated proteomics. Reviewed International journal
Chiaki Yaeshima, Natsumi Murata, Sonoko Ishino, Ikuko Sagawa, Kosuke Ito, Toshio Uchiumi
Biochemical and biophysical research communications 593 116 - 121 2022.2
Structural insights into the Switching Off of the Interaction between the Archaeal Ribosomal Stalk and aEF1A by Nucleotide Exchange Factor aEF1B. Reviewed International journal
Suzuki T, Ito K, Miyoshi T, Murakami R, Uchiumi T
Journal of molecular biology 433 ( 15 ) 167046 - 167046 2021.7
Crystal structure of rice defensin OsAFP1 and molecular insight into lipid-binding. Reviewed
Ochiai A, Ogawa K, Fukuda M, Suzuki M, Ito K, Tanaka T, Sagehashi Y, Taniguchi M
Journal of bioscience and bioengineering 130 ( 1 ) 6 - 13 2020.7
Arabidopsis ROOT PHOTOTROPISM2 Is a Light-Dependent Dynamic Modulator of Phototropin1. Reviewed International journal
Kimura T, Tsuchida-Mayama T, Imai H, Okajima K, Ito K, Sakai T
The Plant Cell 10.1101/862649 2020.3
Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations. Reviewed
Maruyama K, Imai H, Kawamura M, Ishino S, Ishino Y, Ito K, Uchiumi T
Scientific reports 9 ( 1 ) 14761 2019.10
Structural and Mutagenesis Studies Evince the Role of the Extended Protuberant Domain of Ribosomal Protein uL10 in Protein Translation. Reviewed
Choi KA, Yang L, Lee KM, Yu CW, Banfield DK, Ito K, Uchiumi T, Wong KB
Biochemistry 58 ( 36 ) 3744 - 3754 2019.9
High-resolution crystal structure of peptidyl-tRNA hydrolase from Thermus thermophilus. Reviewed International journal
Matsumoto A, Uehara Y, Shimizu Y, Ueda T, Uchiumi T, Ito K
Proteins 87 ( 3 ) 226 - 235 2019.3
The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1. Reviewed International journal
Imai H, Abe T, Miyoshi T, Nishikawa SI, Ito K, Uchiumi T
Nucleic acids research 46 ( 15 ) 7820 - 7830 2018.9
The Interaction between the Ribosomal Stalk Proteins and Translation Initiation Factor 5B Promotes Translation Initiation. Reviewed International journal
Murakami R, Singh CR, Morris J, Tang L, Harmon I, Takasu A, Miyoshi T, Ito K, Asano K, Uchiumi T, ibute, Corresponding authors
Molecular and cellular biology 38 ( 16 ) e00067-18 2018.8
Binding of translation elongation factors to individual copies of the archaeal ribosomal stalk protein aP1 assembled onto aP0 Reviewed
Takayoshi Honda, Hirotatsu Imai, Takahiro Suzuki, Tomohiro Miyoshi, Kosuke Ito, Toshio Uchiumi
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 483 ( 1 ) 153 - 158 2017.1
Structural basis for the recognition of guide RNA and target DNA heteroduplex by Argonaute Reviewed
*Miyoshi T, *Ito K, Murakami R, Uchiumi T
NATURE COMMUNICATIONS 7 11846 2016.6
Crystal structure of translation initiation factor 5B from the crenarchaeon Aeropyrum pernix Reviewed
Ryo Murakami, Tomohiro Miyoshi, Toshio Uchiumi, Kosuke Ito
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 84 ( 5 ) 712 - 717 2016.5
Functional role of the C-terminal tail of the archaeal ribosomal stalk in recruitment of two elongation factors to the sarcin/ricin loop of 23S rRNA Reviewed
Imai H, Miyoshi T, Murakami R, Ito K, Ishino Y, Uchiumi T
GENES TO CELLS 20 ( 7 ) 613 - 624 2015.7
Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1 alpha Reviewed
Kosuke Ito, Takayoshi Honda, Takahiro Suzuki, Tomohiro Miyoshi, Ryo Murakami, Min Yao, Toshio Uchiumi
NUCLEIC ACIDS RESEARCH 42 ( 22 ) 14042 - 14052 2014.12
Crystal structure of alpha-amylase from Oryza sativa: molecular insights into enzyme activity and thermostability Reviewed
Akihito Ochiai, Hiroshi Sugai, Kazuki Harada, Seiya Tanaka, Yohei Ishiyama, Kosuke Ito, Takaaki Tanaka, Toshio Uchiumi, Masayuki Taniguchi, Toshiaki Mitsui
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 78 ( 6 ) 989 - 997 2014.6
Solution structure of human P1 center dot P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome Reviewed
Ka-Ming Lee, Kazuyuki Yusa, Lai-On Chu, Conny Wing-Heng Yu, Moe Oono, Tomohiro Miyoshi, Kosuke Ito, Pang-Chui Shaw, Kam-Bo Wong, Toshio Uchiumi
NUCLEIC ACIDS RESEARCH 41 ( 18 ) 8776 - 8787 2013.10
Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8 Reviewed
Matsumoto A, Shimizu Y, Takemoto C, Ueda T, Uchiumi T, *Ito K (*責任著者)
Acta Crystallographica Section F: Structural Biology and Crystallization Communications 69 ( 3 ) 332 - 335 2013.3
Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase Reviewed
Kosuke Ito, Ryo Murakami, Masahiro Mochizuki, Hao Qi, Yoshihiro Shimizu, Kin-ichiro Miura, Takuya Ueda, Toshio Uchiumi
NUCLEIC ACIDS RESEARCH 40 ( 20 ) 10521 - 10531 2012.11
Analysis of chimeric ribosomal stalk complexes from eukaryotic and bacterial sources: structural features responsible for specificity of translation factors Reviewed
Masahiro Mochizuki, Masumi Kitamyo, Tomohiro Miyoshi, Kosuke Ito, Toshio Uchiumi
GENES TO CELLS 17 ( 4 ) 273 - 284 2012.4
Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-T?C domain of tRNA Reviewed
Kosuke Ito, Hao Qi, Yoshihiro Shimizu, Ryo Murakami, Kin-ichiro Miura, Takuya Ueda, Toshio Uchiumi
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 67 ( Pt 12 ) 1566 - 1569 2011.12
Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis Reviewed
Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M
JOURNAL OF BIOLOGICAL CHEMISTRY 283 ( 20 ) 13889 - 13896 2008.5
The structure and reaction mechanism of azoreductase Invited
Ito K, Tanokura M
Seikagaku 80 ( 6 ) 550 - 559 2008
Crystal structure of thioredoxin domain of ST2123 from thermophilic archaea Sulfalabus tokodaii strain7 Reviewed
Hua Ming, Yusuke Kato, Ken-ichi Miyazono, Kosuke Ito, Masayuki Kamo, Koji Nagata, Masaru Tanokura
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 69 ( 1 ) 204 - 208 2007.10
Three-dimensional structure of AzoR from Escherichia coli - An oxidereductase conserved in microorganisms Reviewed
Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M
JOURNAL OF BIOLOGICAL CHEMISTRY 281 ( 29 ) 20567 - 20576 2006.7
Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop Reviewed
Nagata K, Sasaki H, Ohtsuka J, Hua M, Okai M, Kubota K, Kamo M, Ito K, Ichikawa T, Koyama Y, Tanokura M
Proceedings of the Japan Academy Series B: Physical and Biological Sciences 81 ( 6 ) 220 - 224 2005.6
Crystal structure of azoreductase AzoR from Escherichia coli Reviewed
Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M
Proceedings of the Japan Academy Series B: Physical and Biological Sciences 81 ( 6 ) 225 - 228 2005.6
Recombinant porcine zona pellucida glycoproteins expressed in Sf9 cells bind to bovine sperm but not to porcine sperm Reviewed
N Yonezawa, K Kudo, H Terauchi, S Kanai, N Yoda, M Tanokura, K Ito, K Miura, T Katsumata, M Nakano
JOURNAL OF BIOLOGICAL CHEMISTRY 280 ( 21 ) 20189 - 20196 2005.5
Crystallization and preliminary X-ray analysis of AzoR (azoreductase) from Escherichia coli Reviewed
K Ito, M Nakanishi, WC Lee, H Sasaki, S Zenno, K Saigo, Y Kitade, M Tanokura
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 61 ( Pt 4 ) 399 - 402 2005.4
Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus Reviewed
K Nagata, S Tsutsui, WC Lee, K Ito, M Kamo, Y Inoue, M Tanokura
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 60 ( 8 ) 1445 - 1446 2004.8
Flavins and Flavoproteins
Nishino T, Miura R, Tanokura M, Fukui K. ed( Role: Joint author)
ARchiTect inc. Tokyo 2005.11
「食品の科学」
上野川修一, 田之倉優( Role: Joint author)
東京化学同人 2005.3
「ナノバイオテクノロジーの最前線」
植田充美( Role: Joint author)
シーエムシー出版 2003.10
「動物細胞工学ハンドブック」
動物細胞工学会編( Role: Joint author)
朝倉書店 2000.10
ペプチジルtRNA加水分解酵素・プロテアソーム輸送タンパク質複合体のX線結晶構造解析
市邨晃久, 笠原杏子, 今井大達, 上原祐二, 西川周一, 内海利男, 伊東孝祐
日本分子生物学会年会プログラム・要旨集(Web) 41st 2018
イネ由来α-アミラーゼの立体構造とその熱安定性に関与する構造要因の解析
落合秋人, 菅井寛, 伊東孝祐, 内海利男, 田中孝明, 谷口正之, 三ツ井敏明
日本生化学会大会(Web) 87th 2014
2P-042 Crystal Structure of α-Amylase AmyI-1 from Oryza sativa
Ochiai Akihito, Sugai Hiroshi, Harada Kazuki, Itoh Kousuke, Uchiumi Toshio, Tanaka Takaaki, Taniguchi Masayuki, Mitsui Toshiaki
66 117 - 117 2014
高度好熱菌T.thermophilusペプチジルtRNA加水分解酵素のX線結晶構造解析
松本愛弥, 伊東孝祐, 竹本千重, 内海利男
日本分子生物学会年会プログラム・要旨集(Web) 34th 2011
アゾ還元酵素の構造と反応機構
伊東孝祐, 田之倉優
生化学 80 ( 6 ) 550 - 559 2008.6
Expression of Xenopus laevis translation initiation factor 4E (eIF-4E) by baculovirus-insect cell system.
Miyoshi H, Ito K, Sakai N, Mizushima J, Okamoto K, Hori H, Nishino T, Wakiyama M, Miura K
Nucleic Acids Symposium Series 37 191 - 192 1997.12
抗原結合用キャリア及びその使用
内海利男, 須田真広, 藤間真紀, 伊東孝祐
B.B.B.論文賞
2015.3 日本農芸化学会
Ochiai A, Sugai H, Harada K, Tanaka S, Ishiyama Y, Ito K, Tanaka T, Uchiumi T, Taniguchi M, Mitsui T
結核菌の休眠誘導の構造基盤解明
Grant number:23H02417
2023.4 - 2026.3
System name:科学研究費助成事業 基盤研究(B)
Research category:基盤研究(B)
Awarding organization:日本学術振興会
伊東 孝祐, 松本 壮吉, 真柳 浩太
Grant amount:\18720000 ( Direct Cost: \14400000 、 Indirect Cost:\4320000 )
天然変性蛋白質(IDP)を標的とする、中分子化合物による、新しい創薬フィールドの開拓
2022.10 - 2028.3
System name:革新的先端研究開発支援事業 感染症創薬基盤研究開発領域
Research category:感染症創薬基盤研究開発領域
Awarding organization:日本医療研究開発機構
松本 壮吉, 古寺 哲幸, 伊東 孝祐, 西山 晃史, 真柳 浩太, 廣明 秀一, 岩本 啓, 白井 剛
Authorship:Coinvestigator(s)
生態系保全のための新規抗結核薬の開発研究
Grant number:14861
2022.7 - 2024.3
System name:試験研究費助成
Awarding organization:佐々木環境技術振興財団
伊東孝祐
Authorship:Principal investigator
次世代型環境浄化酵素生産システムの開発 (リボソームのエネルギー代謝中心部位の改良研究)
Grant number:R04-1-019
2022.7 - 2023.3
System name:試験研究費助成
Awarding organization:財団法人内田エネルギー科学振興財団
伊東孝祐
Authorship:Principal investigator
Elucidation of the relationship between protein synthesis system and protein degradation system
Grant number:22K19267
2022.6 - 2025.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Research (Exploratory)
Research category:Grant-in-Aid for Challenging Research (Exploratory)
Awarding organization:Japan Society for the Promotion of Science
Grant amount:\6370000 ( Direct Cost: \4900000 、 Indirect Cost:\1470000 )
休眠結核菌を殺傷する薬剤の開発
2022.6 - 2023.3
System name:科学技術研究費助成金制度
Awarding organization:公益財団法人ユニオンツール育英奨学会
伊東孝祐
Authorship:Principal investigator
Development of Next-Generation Platform for Light-induced Drugs
Grant number:20K21541
2020.7 - 2023.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Research (Exploratory)
Research category:Grant-in-Aid for Challenging Research (Exploratory)
Awarding organization:Japan Society for the Promotion of Science
Grant amount:\6370000 ( Direct Cost: \4900000 、 Indirect Cost:\1470000 )
Development of CRISPR-Cas-type antibacterial agents specifically targeting MRSA
Grant number:20K21671
2020.7 - 2022.3
System name:Grants-in-Aid for Scientific Research
Research category:Grant-in-Aid for Challenging Research (Exploratory)
Awarding organization:Japan Society for the Promotion of Science
Terao Yutaka
Grant amount:\6500000 ( Direct Cost: \5000000 、 Indirect Cost:\1500000 )
The estimated death by MRSA infections in Japan is more than 10,000 per year. Furthermore, in the latest infection control surveillance, the MRSA detection rate at domestic medical institutions was approximately 100%. Nevertheless, research and development of new drugs against drug-resistant bacteria is facing the reality of inadequacy. Therefore, in this present study, we applied CRISPR-Cas genome editing technology to develop a DNA antibacterial drug that specifically deletes the resistance factor PBP2' in MRSA. By using DNA (CRISPR-Cas expression plasmid) as a material, the possibility of side reactions will be low, and the drug target will be able to exchange simply by changing the guide RNA sequence according to the evolution of resistance. This was because it could be an antibacterial drug.
天然変性ヒストン様蛋白質による、結核菌の個性の創出と多様性獲得の分子機構
Grant number:20H03483
2020.4 - 2024.3
System name:科学研究費助成事業 基盤研究(B)
Research category:基盤研究(B)
Awarding organization:日本学術振興会
松本 壮吉, 白井 剛, 伊東 孝祐, 真柳 浩太
Grant amount:\17680000 ( Direct Cost: \13600000 、 Indirect Cost:\4080000 )
Versatile molecular functions of the ribosomal stalk protein in translation cycle
Grant number:19H03155
2019.4 - 2022.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)
Research category:Grant-in-Aid for Scientific Research (B)
Awarding organization:Japan Society for the Promotion of Science
Uchiumi Toshio
Grant amount:\17550000 ( Direct Cost: \13500000 、 Indirect Cost:\4050000 )
Translation of genetic information proceeds on the ribosome with amino acids being brought efficiently to the ribosome by the translation factor EF1A one after another. There are many unclear points about the mechanism for achieving the high efficiency. In this project, we have demonstrated that the ribosomal stalk protein contributes to translation efficiency by binding, via its C-terminal region, to two different conformations of EF1A, that is, the active EF1A-GTP form that carries the aminoacyl-tRNA to the ribosome and the inactive EF1A-GDP form that is dissociated from the ribosome, and that the interaction between the stalk and EF1A is disrupted by anothor factor EF1B which promote nucleotide exchange from EF1A-GDP to EF1A-GTP. Furthermore, we also detected ability of the stalk to bind to a stress-response factor, YchF. These results represent the versatile functions of the ribosomal stalk in translation efficiency and control.
Elucidation of the mechanism of peptidyl-tRNA hydrolysis in the stalled eukaryotic ribosome
Grant number:18K06080
2018.4 - 2021.3
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
Ito Kosuke
Authorship:Principal investigator Grant type:Competitive
Grant amount:\4420000 ( Direct Cost: \3400000 、 Indirect Cost:\1020000 )
During the course of protein synthesis, ribosomes occasionally stall due to various reasons and thus produce peptidyl-tRNAs, which are immature translation products. This unfavorable situation is solved by hydrolyzing the peptidyl-tRNA into the peptide and tRNA components. However, the mechanism of the peptidyl-tRNA hydrolysis in the stalled ribosome still remains unclear in eukaryotes. Our study revealed that Vms1 is not sufficient to hydrolyze the peptidyl-tRNA in the stalled ribosome. We also clarified the structural basis of the substrate recognition and the hydrolysis reaction of Pth, which acts in the cytosol to hydrolyze the peptidyl-tRNAs.
水環境汚染問題解決を目指した新規抗生物質開発研究
2017 - 2019
System name:試験研究費助成
Awarding organization:佐々木環境技術振興財団
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
Functional role of the ribosomal stalk protein in translation recycling
Grant number:16H04741
2016.4 - 2019.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)
Research category:Grant-in-Aid for Scientific Research (B)
Awarding organization:Japan Society for the Promotion of Science
Uchiumi Toshio, IMAI Hirotatsu
Grant type:Competitive
Grant amount:\17420000 ( Direct Cost: \13400000 、 Indirect Cost:\4020000 )
Translation of genetic information, i.e., protein synthesis, on a macromolecular complex called the ribosome occurs in four stages: initiation, elongation, termination, and recycling. So far in research, much less is known about mechanism of the recycling. In this project, we have focused on a ribosome recycling factor, ABCE1 (ATPase), and investigated molecular mechanism of the action of ABCE1 by using techniques of biochemistry and structural biology. As results, we have clarified that a ribosomal protein component, termed the “stalk”, directly binds to a specific site of ABCE1, recruits it to the functional site within the ribosome, and stimulates ATP hydrolysis. Thus, our results demonstrate that interaction between ABCE1 and the stalk protein leads to dissociation of ribosomes to subunits, or ribosome recycling.
Research for the mechanism of DNA silencing using small RNA as a guide strand
Grant number:16K07246
2016.4 - 2019.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)
Research category:Grant-in-Aid for Scientific Research (C)
Awarding organization:Japan Society for the Promotion of Science
Miyoshi Tomohiro
Grant type:Competitive
Grant amount:\4940000 ( Direct Cost: \3800000 、 Indirect Cost:\1140000 )
Argonaute (RsAgo) of Rhodobacter sphaeroides binds in a sequence-specific manner to a target DNA using small RNA as a guide strand. RsAgo is an important protein involved in the development of new gene analysis technology. In this study, the new results were obtained regarding (1) guide strand selection mechanisms of RsAgo, (2) the influence of each domain structure on nucleic acid recognition and function, and (3) the functional role of DNA silencing.
Grant number:15K06964
2015.4 - 2018.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)
Research category:Grant-in-Aid for Scientific Research (C)
Awarding organization:Japan Society for the Promotion of Science
Kosuke Ito, UCHIUMI Toshio
Authorship:Principal investigator Grant type:Competitive
Grant amount:\4940000 ( Direct Cost: \3800000 、 Indirect Cost:\1140000 )
The ribosomal stalk protein moves in a broad range on the ribosome. The ribosomal stalk protein directly interacts with and recruits the translation factors to the ribosome. On the other hand, recently it was found that the ribosomal stalk protein also binds to aminoacyl-tRNA synthetase and contributes to the efficient supply of aminoacyl-tRNA to the translation elongation factor. In our present research, we first conducted the analysis of the interaction between the ribosomal stalk protein and aminoacyl-tRNA synthetase. The results suggested that the N-terminal region of the C-terminal domain of the stalk protein is important for the binding. In addition, we obtained the microcrystals of the stalk protein-aminoacyl-tRNA complex.
環境浄化酵素生産システムの開発
2013 - 2014
System name:試験研究費助成
Awarding organization:佐々木環境技術振興財団
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
Grant number:24370073
2012.4 - 2015.3
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)
Research category:Grant-in-Aid for Scientific Research (B)
Awarding organization:Japan Society for the Promotion of Science
UCHIUMI Toshio, ITO Kosuke, YAO Minn, MIYOSHI Tomohiro, UCHIYAMA Susumu
Grant type:Competitive
Grant amount:\18330000 ( Direct Cost: \14100000 、 Indirect Cost:\4230000 )
We have studied on the ribosomal stalk protein complex, which determines the rate and efficiency of protein synthesis (translation), by using biochemical and crystallographic approaches, as follows: 1) multiple copies of the stalk proteins all bind to the ribosomal core via their N-terminal domains, and the C-terminal region of each stalk is flexible and moving widely around the ribosome; 2) the crystal structural data indicate that the C-terminal region of the stalk protein binds to individual translation factors through hydrophobic interactions; 3) the interactions between the C-terminal region of the stalk protein and translation factors is important to recruit the factors to the functional center within the ribosomal core. These lines of evidence demonstrate the crucial contribution of the stalk protein to efficient translation.
tRNA再生酵素-基質複合体のX線結晶構造解析
2012 - 2015
System name:若手研究(B)
Research category:若手研究(B)
Awarding organization:日本学術振興会
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
Creation of the tailor-made system for antibody production by using an autoantigenic complex
Grant number:23657087
2011 - 2013
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research
Research category:Grant-in-Aid for Challenging Exploratory Research
Awarding organization:Japan Society for the Promotion of Science
UCHIUMI Toshio, ITO Koshuke, AOYAGI Yutaka
Grant type:Competitive
Grant amount:\3900000 ( Direct Cost: \3000000 、 Indirect Cost:\900000 )
The aim of this study is to clarify the relationship between the structure and antigenicity of ribosomal autoantigen (P0-P1-P2 complex), and to develop a useful antibody-production system. Epitope analysis of the ribosomal autoantigen identified the 3 amino acids at the C-terminus, which is shared by P0/P1/P2 and responsible for anti-P recognition. It was also found that phosphorylation at Ser residues adjacent to the 3 amino acids enhanced the anti-P binding, suggesting that phosphorylation of the autoantigen is related to the antigenicity. We also found that aP1, the archaeal homologue of human P1/P2, forms a stable tetramer and that immunization of this tetramer resulted in production of antibodies to the conserved C-terminal part. When the C-terminal amino acid sequence was replaced with a sequence of another ribosomal protein, the antibody specific to the introduced sequence was produced. We thus developed a novel method to produce efficiently the antibody for a desired sequence.
タンパク質生合成系の保守管理を担うペプチジルtRNA分解酵素の分子機構解明
2011 - 2012
System name:科学技術研究費助成金制度
Awarding organization:ユニオンツール育英奨学会
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
Grant number:21370078
2009 - 2011
System name:Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)
Research category:Grant-in-Aid for Scientific Research (B)
Awarding organization:Japan Society for the Promotion of Science
UCHIUMI Toshio, ITO Kosuke, YAO Minn
Grant amount:\18590000 ( Direct Cost: \14300000 、 Indirect Cost:\4290000 )
Ribosomes in all organisms have a unique flexible structure composed of ribosomal protein complex, termed the stalk, which plays a crucial role in ribosome function. In this research subject, we have investigated the structure and function of the ribosomal stalk in a hyperthermophilic archaeon by biochemical and crystallographic analyses. The results showed that the archaeal stalk is composed of aP0 and aP1, which form the heptameric complex aP0(aP1)_2(aP1)_2(aP1)_2, and that the C-terminal sequence, which is shared by aP1 and aP0, directly binds to translation factors. We concluded that the 7 copies of C-terminal tails of aP1/aP0 in the complex participate in efficient recruitment of translation factors onto the ribosome.
リボソーム結合性GTPaseファミリーの構造生物学
2009 - 2011
System name:若手研究(B)
Research category:若手研究(B)
Awarding organization:日本学術振興会
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
タンパク質合成システムにおけるエネルギー代謝中心の機能制御研究
2009 - 2010
System name:研究助成
Awarding organization:財団法人内田エネルギー科学振興財団
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
超高熱古細菌リボソームストークタンパク質とGTP結合翻訳因子の構造・機能研究
2008 - 2009
System name:若手研究 (スタートアップ)
Research category:若手研究(スタートアップ)
Awarding organization:日本学術振興会
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
タンパク質低速合成大腸菌株AM68を利用した有用タンパク質生産システムの開発
2008 - 2009
System name:シーズ発掘試験A(発掘型)
Awarding organization:科学技術振興機構
伊東孝祐
Authorship:Principal investigator Grant type:Competitive
細胞生物学演習
生命・食料科学特定研究BⅡ
文献詳読Ⅱ
課題研究II
生命科学への招待(生物学学習法)
基礎生物科学実習II
自然科学基礎実験
細胞生物学Ⅰ
生物学基礎実習a
理学スタディ・スキルズ
生物学基礎演習
総合力アクティブ・ラーニング
生物学実習
生体分子機能学実習
研究発表演習(中間発表)
生命・食料科学セミナーBⅠ
生命・食料科学特定研究BⅠ
生物学実験 I
文献詳読Ⅰ
原書講読
生命・食料科学セミナーBⅡ
基礎生物科学実習I
生物化学実習
課題研究I(生物学科)
生物英語I
生物英語
生体情報学I
生物学実習IV
生物学実習I
生体情報学
生物学基礎B
自然科学総論IV
基礎生物科学実習I
基礎生物科学実習II
構造生物学特論
領域概説 B (理学)
リフレクションデザインIII
リフレクションデザインII
生物学実験
タンパク質・核酸化学特論
構造生物学特論
先端科学技術総論
生物学特論 V
細胞生物学I
タンパク質・核酸化学特論
日本事情自然系A
自然科学基礎実験
課題研究II(生物学)
理学スタディ・スキルズ
課題研究I(生物学)
生物学総合演習
生物学基礎実習a
総合力アクティブ・ラーニング
生物学特論I
生物学基礎演習
生体分子機能学実習
基礎生物科学実習II
生物学実習
生命科学への招待(生物学学習法)
生物英語I
細胞生物学演習
基礎生物科学実習I
生命・食料科学セミナーBⅡ
生物化学実習
生命・食料科学特定研究BⅡ
文献詳読Ⅱ
研究発表演習(中間発表)
課題研究I(生物学科)
課題研究II
生命・食料科学セミナーBⅠ
文献詳読Ⅰ
生命・食料科学特定研究BⅠ
原書講読
生物学実験 I
新潟大学公開講座「目指せ!未来の科学者」
Role(s): Lecturer
2018.9 - 2018.10
独立行政法人科学技術振興機構「未来の科学者養成講座」
Role(s): Lecturer
2011.9 - 2012.3
新潟県内外高等学校 出前授業
Role(s): Lecturer
2011
新聞報道:「遺伝子解析へ新手法」
新潟日報新聞 2016.8
新聞報道:「イネの主要α-アミラーゼ立体構造を解明」
科学新聞 2014.8
新聞報道:「アゾ還元酵素解明」
科学新聞 2006.8
新聞報道:「東大、環境を汚染する合成色素を浄化する酵素の立体構造を解明」
日刊工業新聞 2006.7