Updated on 2024/06/22

写真a

 
HAYASHI Yasuko
 
Organization
Academic Assembly Institute of Science and Technology CHIKYU SEIBUTSU KAGAKU KEIRETU Associate Professor
Graduate School of Science and Technology Environmental Science and Technology Associate Professor
Faculty of Science Department of Science Associate Professor
Title
Associate Professor
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Degree

  • 理学博士 ( 1994.1   奈良女子大学 )

Research Interests

  • ミトコンドリア

  • ペルオキシソーム

  • 超微形態機能学

  • 電子顕微鏡

  • 子葉

  • 緑藻

  • オルガネラ

Research Areas

  • Life Science / Cell biology

Research History (researchmap)

  • Niigata University   Faculty of Science Department of Science   Associate Professor

    2017.4

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    Country:Japan

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  • Niigata University   Graduate School of Science and Technology Environmental Science and Technology   Associate Professor

    2010.4

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  • Niigata University   Faculty of Science Department of Environmental Science   Associate Professor

    2004.4 - 2022.3

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  • Niigata University   Faculty of Science Department of Environmental Science Environmental Biology   Associate Professor (as old post name)

    2001.3 - 2004.3

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  • 基礎生物学研究所日本学術振興会未来開拓学術推進事業   研究員

    1997.7 - 2001.3

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  • ロックフェラー大学   ポストドクトラルフェロー

    1995.11 - 1997.7

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  • JT関連会社 生命誌研究館   研究員

    1994.4 - 1995.10

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  • Nara Women's University   Faculty of Science   Research Assistant

    1990.4 - 1994.3

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Research History

  • Niigata University   Faculty of Science Department of Science   Associate Professor

    2017.4

  • Niigata University   Graduate School of Science and Technology Environmental Science and Technology   Associate Professor

    2010.4

  • Niigata University   Graduate School of Science and Technology Environmental Science and Technology   Associate Professor

    2010.4

  • Niigata University   Faculty of Science Department of Environmental Science   Associate Professor

    2004.4 - 2017.3

  • Niigata University   Abolition organization Environmental Biology   Associate Professor (as old post name)

    2001.3 - 2004.3

Professional Memberships

  • THE JAPANESE SOCIETY OF PLANT MORPHOLOGY

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  • THE JAPANESE SOCIETY OF PLANT PHYSIOLOGISTS

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  • THE BOTANICAL SOCIETY OF JAPAN

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  • THE JAPANESE SOCIETY OF PHYCOLOGY

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Committee Memberships

  • 日本植物形態学会   評議員  

    2024.1   

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  • 日本植物形態学会   庶務幹事  

    2022.1 - 2023.12   

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    Committee type:Academic society

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  • 日本植物形態学会   評議員  

    2018.1 - 2019.12   

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  • 日本植物生理学会   評議員  

    2014.1 - 2015.12   

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  • 日本植物形態学会   会計幹事  

    2012.1 - 2018.12   

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  • 日本植物生理学会   評議員  

    2006.1 - 2007.12   

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Papers

  • Pexophagy in plants: a mechanism to remit cells from oxidative damage caused under high-intensity light. Reviewed International journal

    Shino Goto-Yamada, Kazusato Oikawa, Yasuko Hayashi, Shoji Mano, Kenji Yamada, Mikio Nishimura

    Autophagy   19 ( 5 )   1611 - 1613   2023.3

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

    Light is essential for plant growth, but excessive light energy produces reactive oxygen species (ROS), which can seriously damage cells. Mutants defective in ATG (autophagy related) genes show light intensity-dependent leaf damage and ROS accumulation. We found that autophagy is one of the crucial systems in protecting plants from ROS-induced damage by removing oxidative peroxisomes. Damaged peroxisomes are targeted by the PtdIns3P marker and specifically engulfed by phagophores labeled by ATG18a-GFP. Under high-intensity light, huge peroxisome aggregates are induced and captured by vacuolar membranes. Research provides a deeper understanding of plant stress response to light irradiation.

    DOI: 10.1080/15548627.2023.2175570

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  • Pexophagy suppresses ROS-induced damage in leaf cells under high-intensity light. Reviewed International journal

    Kazusato Oikawa, Shino Goto-Yamada, Yasuko Hayashi, Daisuke Takahashi, Yoshitaka Kimori, Michitaro Shibata, Kohki Yoshimoto, Atsushi Takemiya, Maki Kondo, Kazumi Hikino, Akira Kato, Keisuke Shimoda, Haruko Ueda, Matsuo Uemura, Keiji Numata, Yoshinori Ohsumi, Ikuko Hara-Nishimura, Shoji Mano, Kenji Yamada, Mikio Nishimura

    Nature communications   13 ( 1 )   7493 - 7493   2022.12

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    Although light is essential for photosynthesis, it has the potential to elevate intracellular levels of reactive oxygen species (ROS). Since high ROS levels are cytotoxic, plants must alleviate such damage. However, the cellular mechanism underlying ROS-induced leaf damage alleviation in peroxisomes was not fully explored. Here, we show that autophagy plays a pivotal role in the selective removal of ROS-generating peroxisomes, which protects plants from oxidative damage during photosynthesis. We present evidence that autophagy-deficient mutants show light intensity-dependent leaf damage and excess aggregation of ROS-accumulating peroxisomes. The peroxisome aggregates are specifically engulfed by pre-autophagosomal structures and vacuolar membranes in both leaf cells and isolated vacuoles, but they are not degraded in mutants. ATG18a-GFP and GFP-2×FYVE, which bind to phosphatidylinositol 3-phosphate, preferentially target the peroxisomal membranes and pre-autophagosomal structures near peroxisomes in ROS-accumulating cells under high-intensity light. Our findings provide deeper insights into the plant stress response caused by light irradiation.

    DOI: 10.1038/s41467-022-35138-z

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  • Ubiquitin-conjugating activity by PEX4 is required for efficient protein transport to peroxisomes in Arabidopsis thaliana Reviewed International journal

    Shoji Mano, Yasuko Hayashi, Kazumi Hikino, Masayoshi Otomo, Masatake Kanai, Mikio Nishimura

    Journal of Biological Chemistry   298 ( 6 )   102038 - 102038   2022.6

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

    Protein transport to peroxisomes requires various proteins, such as receptors in the cytosol and components of the transport machinery on peroxisomal membranes. The Arabidopsis apem (aberrant peroxisome morphology) mutant apem7 shows decreased efficiency of peroxisome targeting signal 1-dependent protein transport to peroxisomes. In apem7 mutants, peroxisome targeting signal 2-dependent protein transport is also disturbed, and plant growth is repressed. The APEM7 gene encodes a protein homologous to peroxin 4 (PEX4), which belongs to the ubiquitin-conjugating (UBC) protein family; however, the UBC activity of Arabidopsis PEX4 remains to be investigated. Here, we show using electron microscopy and immunoblot analysis using specific PEX4 antibodies and in vitro transcription/translation assay that PEX4 localizes to peroxisomal membranes and possesses UBC activity. We found that the substitution of proline with leucine by apem7 mutation alters ubiquitination of PEX4. Furthermore, substitution of the active-site cysteine residue at position 90 in PEX4, which was predicted to be a ubiquitin-conjugation site, with alanine did not restore the apem7 phenotype. Taken together, these findings indicate that abnormal ubiquitination in the apem7 mutant alters ubiquitin signaling during the process of protein transport, suggesting that the UBC activity of PEX4 is indispensable for efficient protein transport to peroxisomes.

    DOI: 10.1016/j.jbc.2022.102038

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  • A resin cyanoacrylate nanoparticle as an acute cell death inducer to broad spectrum of microalgae Reviewed

    Ayat J.S. Al-Azab, Dwiyantari Widyaningrum, Haruna Hirakawa, Yashuko Hayashi, Satoshi Tanaka, Takeshi Ohama

    Algal Research   54   102191 - 102191   2021.4

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    Publishing type:Research paper (scientific journal)   Publisher:Elsevier BV  

    DOI: 10.1016/j.algal.2021.102191

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  • Re-evaluation of physical interaction between plant peroxisomes and other organellesusing live-cell imaging techniques. Reviewed

    Oikawa K, Hayashi M, Hayashi Y, Nishimura M

    Journal of integrative plant biology   61 ( 7 )   836 - 852   2019.3

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    Language:English   Publisher:WILEY  

    The dynamic behavior of organelles is essential for plant survival under various environmental conditions. Plant organelles, with various functions, migrate along actin filaments and contact other types of organelles, leading to physical interactions at a specific site called the membrane contact site. Recent studies have revealed the importance of physical interactions in maintaining efficient metabolite flow between organelles. In this review, we first summarize peroxisome function under different environmental conditions and growth stages to understand organelle interactions. We then discuss current knowledge regarding the interactions between peroxisome and other organelles, i.e., the oil bodies, chloroplast, and mitochondria from the perspective of metabolic and physiological regulation, with reference to various organelle interactions and techniques for estimating organelle interactions occurring in plant cells.

    DOI: 10.1111/jipb.12805

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  • アクリルナノ粒子が示す広範囲な殺藻 ・増殖抑制と作用メカニズム

    クリーンテクノロジー   29 ( 3 )   1 - 9   2019

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  • Acutely induced cell mortality in the unicellular green alga Chlamydomonas reinhardtii (Chlorophyceae) following exposure to acrylic resin nanoparticles. Reviewed

    Widyaningrum D, Iida D, Tanabe Y, Hayashi Y, Kurniasih SD, Ohama T

    Journal of phycology   55 ( 1 )   118 - 133   2018.10

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    Nanoparticles have unique properties that make them attractive for use in industrial and medical technology industries but can also be harmful to living organisms, making an understanding of their molecular mechanisms of action essential. We examined the effect of three different sized poly(isobutyl-cyanoacrylate) nanoparticles (iBCA-NPs) on the unicellular green alga Chlamydomonas reinhardtii. We found that exposure to iBCA-NPs immediately caused C. reinhardtii to display abnormal swimming behaviors. Furthermore, after one hour, most of the cells had stopped swimming and 10%-30% of cells were stained with trypan blue, suggesting that these cells had severely impaired plasma membranes. Observation of the cyto-ultrastructure showed that the cell walls had been severely damaged and that many iBCA-NPs were located in the space between the cell wall and plasma membrane, as well as inside the cytosol in some cases. A comparison of three strains of C. reinhardtii with different cell wall conditions further showed that the cell mortality ratio increased more rapidly in the absence of a cell wall. Interestingly, cell mortality over time was essentially identical regardless of iBCA-NP size if the total surface area was the same. Furthermore, direct observation of the trails of iBCA-NPs indicated that the first trigger was their contact with the cell wall, which is most likely accompanied by the inactivation or removal of adsorbed proteins from the cell wall surface. Cell mortality was accompanied by the overproduction of reactive oxygen species, which was detected more readily in cells grown under constant light rather than in the dark.

    DOI: 10.1111/jpy.12798

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  • Existence of Lipid Bodies Surrounded by Membranes in Early Greening Cotyledonary Cells Reviewed

    Hayashi Yasuko, Takagi Chinatsu, Nishimura Mikio

    CYTOLOGIA   83 ( 2 )   123 - 123   2018.6

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    Authorship:Lead author, Corresponding author   Language:English   Publisher:UNIV TOKYO CYTOLOGIA  

    DOI: 10.1508/cytologia.83.123

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  • Sucrose Production Mediated by Lipid Metabolism Suppresses the Physical Interaction of Peroxisomes and Oil Bodies during Germination of Arabidopsis thaliana Reviewed

    Songkui Cui, Yasuko Hayashi, Masayoshi Otomo, Shoji Mano, Kazusato Oikawa, Makoto Hayashi, Mikio Nishimura

    JOURNAL OF BIOLOGICAL CHEMISTRY   291 ( 38 )   19734 - 19745   2016.9

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

    Physical interaction between organelles is a flexible event and essential for cells to adapt rapidly to environmental stimuli. Germinating plants utilize oil bodies and peroxisomes to mobilize storage lipids for the generation of sucrose as the main energy source. Although membrane interaction between oil bodies and peroxisomes has been widely observed, its underlying molecular mechanism is largely unknown. Here we present genetic evidence for control of the physical interaction between oil bodies and peroxisomes. We identified alleles of the sdp1 mutant altered in oil body morphology. This mutant accumulates bigger and more oil body aggregates compared with the wild type and showed defects in lipid mobilization during germination. SUGAR DEPENDENT 1 (SDP1) encodes major triacylglycerol lipase in Arabidopsis. Interestingly, sdp1 seedlings show enhanced physical interaction between oil bodies and peroxisomes compared with the wild type, whereas exogenous sucrose supplementation greatly suppresses the interaction. The same phenomenon occurs in the peroxisomal defective 1 (ped1) mutant, defective in lipid mobilization because of impaired peroxisomal -oxidation, indicating that sucrose production is a key factor for oil body-peroxisomal dissociation. Peroxisomal dissociation and subsequent release from oil bodies is dependent on actin filaments. We also show that a peroxisomal ATP binding cassette transporter, PED3, is the potential anchor protein to the membranes of these organelles. Our results provide novel components linking lipid metabolism and oil body-peroxisome interaction whereby sucrose may act as a negative signal for the interaction of oil bodies and peroxisomes to fine-tune lipolysis.

    DOI: 10.1074/jbc.M116.748814

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  • Increase in peroxisome number and the gene expression of putative glyoxysomal enzymes in Chlamydomonas cells supplemented with acetate Reviewed

    Yasuko Hayashi, Nagisa Sato, Akiko Shinozaki, Mariko Watanabe

    JOURNAL OF PLANT RESEARCH   128 ( 1 )   177 - 185   2015.1

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER JAPAN KK  

    We cultured Chlamydomonas reinhardtii cells in a minimal culture medium supplemented with various concentrations of acetate, fatty acids, ethanol, fatty alcohols, or sucrose. The presence of acetate (0.5 or 1.0 %, w/v) was advantageous for cell growth. To determine whether peroxisomes are involved in fatty acid and fatty alcohol metabolism, we investigated the dynamics of peroxisomes, including changes in their number and size, in the presence of acetate, ethanol, and sucrose. The total volume of peroxisomes increased when cells were grown with acetate, but did not change when cells were grown with ethanol or sucrose. We analyzed cell growth on minimal culture medium supplemented with various fatty acids (carbon chain length ranging from one to ten) to investigate which fatty acids are metabolized by C. reinhardtii. Among them, acetate caused the greatest increase in growth when added to minimal culture media. We analyzed the transcript levels of genes encoding putative glyoxysomal enzymes. The transcript levels of genes encoding malate synthase, malate dehydrogenase, isocitrate lyase, and citrate synthase increased when Chlamydomonas cells were grown on minimal culture medium supplemented with acetate. Our results suggest that Chlamydomonas peroxisomes are involved in acetate metabolism via the glyoxylate cycle.

    DOI: 10.1007/s10265-014-0681-8

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  • Proteomic Analysis Reveals That the Rab GTPase RabE1c Is Involved in the Degradation of the Peroxisomal Protein Receptor PEX7 (Peroxin 7) Reviewed

    Songkui Cui, Yoichiro Fukao, Shoji Mano, Kenji Yamada, Makoto Hayashi, Mikio Nishimura

    Journal of Biological Chemistry   288 ( 8 )   6014 - 6023   2013.2

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    Publishing type:Research paper (scientific journal)   Publisher:American Society for Biochemistry & Molecular Biology (ASBMB)  

    DOI: 10.1074/jbc.m112.438143

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  • Visualization of microbodies in Chlamydomonas reinhardtii Reviewed

    Yasuko Hayashi, Akiko Shinozaki

    JOURNAL OF PLANT RESEARCH   125 ( 4 )   579 - 586   2012.7

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER TOKYO  

    In Chlorophycean algal cells, these organelles are generally called microbodies because they lack the enzymes found in the peroxisomes of higher plants. Microbodies in some algae contain fewer enzymes than the peroxisomes of higher plants, and some unicellular green algae in Chlorophyceae such as Chlamydomonas reinhardtii do not possess catalase, an enzyme commonly found in peroxisomes. Thus, whether microbodies in Chlorophycean algae are similar to the peroxisomes of higher plants, and whether they use a similar transport mechanism for the peroxisomal targeting signal (PTS), remain unclear. To determine whether the PTS is present in the microbodies of Chlorophycean algae, and to visualize the microbodies in Chlamydomonas cells, we examined the sub-cellular localization of green fluorescent proteins (GFP) fused to several PTS-like sequences. We detected GFP compartments that were spherical with a diameter of 0.3-1.0 mu m in transgenic Chlamydomonas. Comparative analysis of the character of GFP-compartments observed by fluorescence microscopy and that of microbodies by electron microscopy indicated that the compartments were one and the same. The result also showed that the microbodies in Chlorophycean cells have a similar transport mechanism to that of peroxisomes of higher plants.

    DOI: 10.1007/s10265-011-0469-z

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  • GNOM-LIKE1/ERMO1 and SEC24a/ERMO2 Are Required for Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis thaliana Reviewed

    Ryohei Thomas Nakano, Ryo Matsushima, Haruko Ueda, Kentaro Tamura, Tomoo Shimada, Lixin Li, Yasuko Hayashi, Maki Kondo, Mikio Nishimura, Ikuko Hara-Nishimura

    PLANT CELL   21 ( 11 )   3672 - 3685   2009.11

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    The endoplasmic reticulum (ER) is composed of tubules, sheets, and three-way junctions, resulting in a highly conserved polygonal network in all eukaryotes. The molecular mechanisms responsible for the organization of these structures are obscure. To identify novel factors responsible for ER morphology, we employed a forward genetic approach using a transgenic Arabidopsis thaliana plant (GFP-h) with fluorescently labeled ER. We isolated two mutants with defects in ER morphology and designated them endoplasmic reticulum morphology1 (ermo1) and ermo2. The cells of both mutants developed a number of ER-derived spherical bodies, similar to 1 mu m in diameter, in addition to the typical polygonal network of ER. The spherical bodies were distributed throughout the ermo1 cells, while they formed a large aggregate in ermo2 cells. We identified the responsible gene for ermo1 to be GNOM-LIKE1 (GNL1) and the gene for ermo2 to be SEC24a. Homologs of both GNL1 and SEC24a are involved in membrane trafficking between the ER and Golgi in yeast and animal cells. Our findings, however, suggest that GNL1/ERMO1 and SEC24a/ERMO2 have a novel function in ER morphology in higher plants.

    DOI: 10.1105/tpc.109.068270

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  • Peroxisomal targeting signals in green algae Reviewed International journal

    Akiko Shinozaki, Nagisa Sato, Yasuko Hayashi

    PROTOPLASMA   235 ( 1-4 )   57 - 66   2009.3

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    Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER WIEN  

    Peroxisomal enzymatic proteins contain targeting signals (PTS) to enable their import into peroxisomes. These targeting signals have been identified as PTS1 and PTS2 in mammalian, yeast, and higher plant cells; however, no PTS2-like amino acid sequences have been observed in enzymes from the genome database of Cyanidiochyzon merolae (Bangiophyceae), a primitive red algae. In studies on the evolution of PTS, it is important to know when their sequences came to be the peroxisomal targeting signals for all living organisms. To this end, we identified a number of genes in the genome database of the green algae Chlamydomonas reinhardtii, which contains amino acid sequences similar to those found in plant PTS. In order to determine whether these sequences function as PTS in green algae, we expressed modified green fluorescent proteins (GFP) fused to these putative PTS peptides under the cauliflower mosaic virus 35S promoter. To confirm whether granular structures containing GFP-PTS fusion proteins accumulated in the peroxisomes of Closterium ehrenbergii, we observed these cells after the peroxisomes were stained with 3, 3'-diaminobenzidine. Our results confirm that the GFP-PTS fusion proteins indeed accumulated in the peroxisomes of these green algae. These findings suggest that the peroxisomal transport system for PTS1 and PTS2 is conserved in green algal cells and that our fusion proteins can be used to visualize peroxisomes in live cells.

    DOI: 10.1007/s00709-009-0031-1

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  • Proteomic Identification and Characterization of a Novel Peroxisomal Adenine Nucleotide Transporter Supplying ATP for Fatty Acid beta-Oxidation in Soybean and Arabidopsis Reviewed

    Yuko Arai, Makoto Hayashi, Mikio Nishimura

    PLANT CELL   20 ( 12 )   3227 - 3240   2008.12

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    We have identified the novel protein Glycine max PEROXISOMAL ADENINE NUCLEOTIDE CARRIER (Gm PNC1) by proteomic analyses of peroxisomal membrane proteins using a blue native/SDS-PAGE technique combined with peptide mass fingerprinting. Gm PNC1, and the Arabidopsis thaliana orthologs At PNC1 and At PNC2, were targeted to peroxisomes. Functional integration of Gm PNC1 and At PNC2 into the cytoplasmic membranes of intact Escherichia coli cells revealed ATP and ADP import activities. The amount of Gm PNC1 in cotyledons increased until 5 d after germination under constant darkness and then decreased very rapidly in response to illumination. We investigated the physiological functions of PNC1 in peroxisomal metabolism by analyzing a transgenic Arabidopsis plant in which At PNC1 and At PNC2 expression was suppressed using RNA interference. The pnc1/2i mutant required sucrose for germination and suppressed the degradation of storage lipids during postgerminative growth. These results suggest that PNC1 contributes to the transport of adenine nucleotides that are consumed by reactions that generate acyl-CoA for peroxisomal fatty acid beta-oxidation during postgerminative growth.

    DOI: 10.1105/tpc.108.062877

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  • 高圧凍結および凍結置換法による電子顕微鏡試料作成 Invited Reviewed

    日本作物学会紀事   76   128 - 130   2007

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  • AtVAM3 is required for normal specification of idioblasts, myrosin cells Reviewed

    H Ueda, C Nishiyama, T Shimada, Y Koumoto, Y Hayashi, M Kondo, T Takahashi, Ohtomo, I, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   47 ( 1 )   164 - 175   2006.1

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

    Myrosin cells in Capparales plants are idioblasts that accumulate thioglucoside glucohydrolase (TGG, also called myrosinase), which hydrolyzes glucosinolates to produce toxic compounds for repelling pests. Here, we show that AtVAM3 is involved in development of myrosin cells. It has been shown that yeast VAM3 is a Q.-SNARE that is involved in vesicle transport of vacuolar proteins and vacuolar assembly. We found that two Arabidopsis atvam3 alleles, atvam3-3 and atvain3-4/ssin, accumulate large amounts of TGG1 and TGG2 that are enzymatically active. An immunogold analysis revealed that TGGs were specifically localized in the vacuole of myrosin cells in atvam3 mutants. This result indicates that TGGs are normally transported to vacuoles in these mutants and that AtVAM3 is not essential for vacuolar transport of the proteins. We developed a staining method with Coomassie brilliant blue that detects myrosin cells in whole leaves by their high TGG content. This method showed that atvam3 leaves have a larger number of myrosin cells than do wild-type leaves. Myrosin cells were scattered along leaf veins in wild-type leaves, while they were abnormally distributed in atvam3 leaves. The mutants developed a network of myrosin cells throughout the leaves: myrosin cells were not only distributed continuously along leaf veins, but were also observe independent of leaf veins. The excess of myrosin cells in atvam3 mutants might be responsible for the abnormal abundance of TGGs and the reduction of elongation of inflorescence stems and leaves in these mutants. Our results suggest that AtVAM3 has a plant-specific function in development of myrosin cells.

    DOI: 10.1093/pcp/pci232

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  • The ER body, a novel endoplasmic reticulum-derived structure in Arabidopsis Reviewed

    R Matsushima, Y Hayashi, K Yamada, T Shimada, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   44 ( 7 )   661 - 666   2003.7

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    Plant cells develop various endoplasmic reticulum (ER)-derived structures with specific functions. The ER body, a novel ER-derived compartment in Arabidopsis, is a spindle-shaped structure (similar to10 mum long and similar to1 mum wide) that is surrounded by ribosomes. Similar structures were found in many Brassicaceae plants in the 1960s and 1970s, but their main components and biological functions have remained unknown. ER bodies can be visualized in transgenic Arabidopsis expressing the green fluorescent protein with an ER-retention signal. A large number of ER bodies are observed in cotyledons, hypocotyls and roots of seedlings, but very few are observed in rosette leaves. Recently nail, a mutant that does not develop ER bodies in whole seedlings, was isolated. Analysis of the nail mutant reveals that a P-glucosidase, called PYK10, is the main component of ER bodies. The putative biological function of PYK10 and the inducibility of ER bodies in rosette leaves by wound stress suggest that the ER body functions in the defense against herbivores.

    DOI: 10.1093/pcp/pcg089

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  • PCP Award - A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis Reviewed

    Y Hayashi, K Yamada, T Shimada, R Matsushima, N Nishizawa, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   44 ( 9 )   S24 - S24   2003

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    Authorship:Lead author   Language:English   Publisher:OXFORD UNIV PRESS  

    DOI: 10.1093/pcp/pce144

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  • An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis Reviewed International journal

    R Matsushima, Y Hayashi, M Kondo, T Shimada, M Nishimura, Hara-Nishimura, I

    PLANT PHYSIOLOGY   130 ( 4 )   1807 - 1814   2002.12

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

    The endoplasmic reticulum (ER) body is a characteristic structure derived from ER and is referred to as a proteinase-sorting system that assists the plant cell under various stress conditions. Fluorescent ER bodies were observed in transgenic plants of Arabidopsis expressing green fluorescent protein fused with an ER retention signal. ER bodies were widely distributed in the epidermal cells of whole seedlings. In contrast, rosette leaves had no ER bodies. We found that wound stress induced the formation of many ER bodies in rosette leaves. ER bodies were also induced by treatment with methyl jasmonate (MeJA), a plant hormone involved in the defense against wounding and chewing by insects. The induction of ER bodies was suppressed by ethylene. An electron microscopic analysis showed that typical ER bodies were induced in the non-transgenic rosette leaves treated with MeJA. An experiment using coil and etr1-4 mutant plants showed that the induction of ER bodies was strictly coupled with the signal transduction of MeJA and ethylene. These results suggested that the formation of ER bodies is a novel and unique type of endomembrane system in the response of plant cells to environmental stresses. It is possible that the biological function of ER bodies is related to defense systems in higher plants.

    DOI: 10.1104/pp.009464

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  • Molecular characterization of an Arabidopsis acyl-coenzyme A synthetase localized on glyoxysomal membranes Reviewed International journal

    H Hayashi, L De Bellis, Y Hayashi, K Nito, A Kato, M Hayashi, Hara-Nishimura, I, M Nishimura

    PLANT PHYSIOLOGY   130 ( 4 )   2019 - 2026   2002.12

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    In higher plants, fat-storing seeds utilize storage lipids as a source of energy during germination. To enter the beta-oxidation pathway, fatty acids need to be activated to acyl-coenzyme As (CoAs) by the enzyme acyl-CoA synthetase (ACS; EC 6.2.1.3). Here, we report the characterization of an Arabidopsis cDNA clone encoding for a glyoxysomal acyl-CoA synthetase designated AtLACS6. The cDNA sequence is 2,106 bp long and it encodes a polypeptide of 701 amino acids with a calculated molecular mass of 76,617 D. Analysis of the amino-terminal sequence indicates that acyl-CoA synthetase is synthesized as a larger precursor containing a cleavable amino-terminal presequence so that the mature polypeptide size is 663 amino acids. The presequence shows high similarity to the typical PTS2 (peroxisomal targeting signal 2). The AtLACS6 also shows high amino acid identity to prokaryotic and eukaryotic fatty acyl-CoA synthetases. Immunocytochemical and cell fractionation analyses indicated that the AtLACS6 is localized on glyoxysomal membranes. AtLACS6 was overexpressed in insect cells and purified to near homogeneity. The purified enzyme is particularly active on long-chain fatty acids (C16:0). Results from immunoblot analysis revealed that the expression of both AtLACS6 and beta-oxidation enzymes coincide with fatty acid degradation. These data suggested that AtLACS6 might play a regulatory role both in fatty acid import into glyoxysomes by making a complex with other factors, e.g. PMP70, and in fatty acid beta-oxidation activating the fatty acids.

    DOI: 10.1104/pp.012955

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  • A vacuolar sorting receptor PV72 on the membrane of vesicles that accumulate precursors of seed storage proteins (PAC Vesicles) Reviewed

    T Shimada, E Watanabe, K Tamura, Y Hayashi, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   43 ( 10 )   1086 - 1095   2002.10

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    A novel vesicle, referred to as a precursor-accumulating (PAC) vesicle, mediates the transport of storage protein precursors to protein storage vacuoles in maturing pumpkin seeds. PV72, a type I integral membrane protein with three repeats of epidermal growth factor, was found on the membrane of the PAC vesicles. PV72 had an ability to bind to pro2S albumin, a storage protein precursor, in a Ca2+- dependent manner, via the C-terminal region of pro2S albumin, which was found to function as a vacuolar targeting signal. This implies that PV72 is a vacuolar sorting receptor of the storage protein. PV72 was specifically and transiently accumulated at the middle stage of seed maturation in association with the synthesis of storage proteins. Subcellular fractionation showed that PV72 was also accumulated in the microsomal fraction. A fusion protein consisting of GFP and the transmembrane domain and the cytosolic tail of PV72 was localized in Golgi complex. PV72 in the isolated PAC vesicles had a complex type of oligosaccharide, indicating that PV72 passed though the Golgi complex. These results suggest that PV72 is recycled between PAC vesicles and Golgi complex/post-Golgi compartments. PV72 appears to be responsible for recruiting pro2S albumin molecules from the Golgi complex to the PAC vesicles.

    DOI: 10.1093/pcp/pcf152

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  • Proteomic Analysis of Leaf Peroxisomal Proteins in Greening Cotyledons of Arabidopsis thaliana Reviewed

    Youichiro Fukao, Makoto Hayashi, Mikio Nishimura

    Plant and Cell Physiology   43 ( 7 )   689 - 696   2002.7

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    DOI: 10.1093/pcp/pcf101

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  • A novel membrane protein that is transported to protein storage vacuoles via precursor-accumulating vesicles Reviewed

    N Mitsuhashi, Y Hayashi, Y Koumoto, T Shimada, T Fukasawa-Akada, M Nishimura, Hara-Nishimura, I

    PLANT CELL   13 ( 10 )   2361 - 2372   2001.10

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    A novel protein, MP73, was specifically found on the membrane of protein storage vacuoles of pumpkin seed. MP73 appeared during seed maturation and disappeared rapidly after seed germination, in association with the morphological changes of the protein storage vacuoles. The MP73 precursor deduced from the isolated cDNA was composed of a signal peptide, a 24-kD domain (P24), and the MP73 domain with a putative long alpha -helix of 13 repeats that are rich in glutamic acid and arginine residues. Immunocytochemistry and immunoblot analysis showed that the precursor-accumulating (PAC) vesicles (endoplasmic reticulum-derived vesicles responsible for the transport of storage proteins) accumulated proMP73, but not MP73, on the membranes. Subcellular fractionation of the pulse-labeled maturing seed demonstrated that the proMP73 form with N-linked oligosaccharides was synthesized on the endoplasmic reticulum and then transported to the protein storage vacuoles via PAC vesicles. Tunicamycin treatment of the seed resulted in the efficient deposition of proMP73 lacking the oligosaccharides (proMP73 Delta Psi) into the PAC vesicles but no accumulation of MP73 in vacuoles. Tunicamycin might impede the transport of proMP73 Delta Psi from the PAC vesicles to the vacuoles or might make the unglycosylated protein unstable in the vacuoles. After arrival at protein storage vacuoles, proMP73 was cleaved by the action of a vacuolar enzyme to form a 100-kD complex on the vacuolar membranes. These results suggest that PAC vesicles might mediate the delivery of not only storage proteins but also membrane proteins of the vacuoles.

    DOI: 10.1105/tpc.13.10.2361

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  • A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis Reviewed

    Y Hayashi, K Yamada, T Shimada, R Matsushima, NK Nishizawa, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   42 ( 9 )   894 - 899   2001.9

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    Plants degrade cellular materials during senescence and under various stresses. We report that the precursors of two stress-inducible cysteine proteinases, RD21 and a vacuolar processing enzyme (VPE), are specifically accumulated in similar to0.5 mum diameter x similar to5 mum long bodies in Arabidopsis thaliana. Such bodies have previously been observed in Arabidopsis but their function was not known. They are surrounded with ribosomes and thus are assumed to be directly derived from the endoplasmic reticulum (ER). Therefore, we propose to call them the ER bodies. The ER bodies are observed specifically in the epidermal cells of healthy seedlings. These cells are easily wounded and stressed by the external environment. When the seedlings are stressed with a concentrated salt solution, leading to death of the epidermal cells, the ER bodies start to fuse with each other and with the vacuoles, thereby mediating the delivery of the precursors directly to the vacuoles. This regulated, direct pathway differs from the usual case in which proteinases are transported constitutively from the ER to the Golgi complex and then to vacuoles, with intervention of vesicle-transport machinery, such as a vacuolar-sorting receptor or a syntaxin of the SNARE family. Thus, the ER bodies appear to be a novel proteinase-storing system that assists in cell death under stressed conditions.

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  • Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin.

    Youichiro Fukao, Youichiro Fukao, Yasuko Hayashi, Shoji Mano, Makoto Hayashi, Mikio Nishimura, Mikio Nishimura

    Plant Cell Physiol.   42 ( 8 )   835 - 841   2001.1

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    In order to clarify the peroxisomal membrane proteins (PMPs), we characterized one of the major PMPs, PMP38. The deduced amino acid sequence for its cDNA in Arabidopsis thaliana contained polypeptides with 331 amino acids and had high similarity with those of Homo sapiens PMP34 and Candida boidinii PMP47 known as homologues of mitochondrial ATP/ADP carrier protein. We expected PMP38 to be localized on peroxisomal membranes, because it had the membrane peroxisomal targeting signal. Cell fractionation and immunocytochemical analysis using pumpkin cotyledons revealed that PMP38 is localized on peroxisomal membranes as an integral membrane protein. The amount of PMP38 in pumpkin cotyledons increased and reached the maximum protein level after 6 d in the dark but decreased thereafter. Illumination of the seedlings caused a significant decrease in the amount of the protein. These results clearly showed that the membrane protein PMP38 in glyoxysomes changes dramatically during the transformation of glyoxysomes to leaf peroxisomes, as do the other glyoxysomal enzymes, especially enzymes of the fatty acid β-oxidation cycle, that are localized in the matrix of glyoxysomes.

    DOI: 10.1093/pcp/pce108

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  • Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant Reviewed

    Y Hayashi, M Hayashi, H Hayashi, Hara-Nishimura, I, M Nishimura

    PROTOPLASMA   218 ( 1-2 )   83 - 94   2001

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    During germination and subsequent growth of fatty seeds, higher plants obtain energy from the glyconcogenic pathway in which fatty acids are converted to succinate in glyoxysomes, which contain enzymes for fatty acid beta -oxidation and the glyoxylate cycle. The Arabidopsis thaliana peril gene encodes a 3-ketoacyl-CoA thiolase (EC 2.3.1.16) involved in fatty acid beta -oxidation. The peril mutant shows normal germination and seedling growth under white light. However, etiolated cotyledons of the peril mutant grow poorly in the dark and have small cotyledons. To elucidate the mechanisms of lipid degradation during germination in the peril mutant, we examined the morphology Of the peril mutant. The glyoxysomes in etiolated cotyledons of the peril mutant appeared abnormal, having tubular structures that contained many vesicles. Electron microscopic analysis revealed that the tubular structures in glyoxysomes are derived from invagination of the glyoxysomal membrane. By immunoelectron microscopic analysis, acyl-CoA synthetase (EC 6.2.1.3), which was located on the membrane of glyoxysomes in wildtype plants, was located on the membranes of the tubular structures in the glyoxysomes in the ped1 mutant. These invagination sites were always in contact with lipid bodies. The tubular structure had many vesicles containing substances with the same electron density as those in the lipid bodies. From these results, we propose a model in which there is a direct mechanism of transporting lipids from the lipid bodies to glyoxysomes during fatty acid beta -oxidation.

    DOI: 10.1007/BF01288364

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  • Functional Transformation of Plant Peroxisomes Reviewed

    Makoto Hayashi, Kanako Toriyama, Maki Kondo, Akira Kato, Shoji Mano, Luigi De Bellis, Yasuko Hayashi-Ishimaru, Katsushi Yamaguchi, Hiroshi Hayashi, Mikio Nishimura

    Cell Biochemistry and Biophysics   32   295 - 304   2000

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    Peroxisomes in higher plant cells are known to differentiate into at least three different classes, namely, glyoxysomes, leaf peroxisomes, and unspecialized peroxisomes, depending on the cell types. In germinating fatty seedlings, glyoxysomes that first appear in the etiolated cotyledonary cells are functionally transformed into leaf peroxisomes during greening. Subsequently, the organelles are transformed back into glyoxysomes during senescence of the cotyledons. Flexibility of function is a distinct feature of plant peroxisomes. This article briefly describes recent studies of the regulatory mechanisms involved in the changes of the function of plant peroxisomes.

    DOI: 10.1385/CBB:32:1-3:295

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  • Distribution of the mitochondrial deviant genetic code AUA for methionine in heterokont algae Reviewed

    M Ehara, KI Watanabe, H Kawai, Y Inagaki, Y Hayashi-Ishimaru, T Ohama

    JOURNAL OF PHYCOLOGY   34 ( 6 )   1005 - 1008   1998.12

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    The DNA sequence of the cytochrome oxidase subunit I (COXI) gene (1059 bp), was determined in a number of heterokont algae, including five species of the Phaeophyceae [Chorda filum (Linnaeus) Stackhouse, Colpomenia bullosa (Saunders) Yamada, Ectocarpus sp., Pseudochorda nagaii (Tokida) Inagaki, Undaria pinnatifida (Harvey) Suringar], and a member of the Raphidophyceae [Chattonella antiqua (Hada) Ono]. The distribution of a deviant mitochondrial code, the AUA codon for methionine (AUA/Met), which was previously reported in the Xanthophyceae, was inferred from these COXI sequences. Comparative analyses of these sequences revealed that all the algae described above bear the universal genetic code, including the assignment for the AUA codon. A phylogenetic tree was constructed using the obtained sequences along with already-published COXI sequences of various heterokont algae. The clusters of the Xanthophyceae and the Phaeophyceae were resolved as sister groups with high bootstrap support, excluding a bacillariophycean species, a raphidophycean species, and three species of the Eustigratophyceae. Taking the distribution of the deviant code and the COXI phylogenetic tree together, the genetic code change most probably occurred in an ancestor of the Xanthophyceae after it had branched off from the Phaeophyceae.

    DOI: 10.1046/j.1529-8817.1998.341005.x

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  • Directionally evolving genetic code: the UGA codon from stop to tryptophan in mitochondria. Reviewed

    Inagaki, Y, Ehara, M, Watanabe, KI, Hayashi-Ishimaru, Y, Ohama, T

    Journal of Molecular Evolution   47 ( 4 )   378-384 - 384   1998.10

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  • A deviant mitochondrial genetic code in prymnesiophytes (yellow-algae): UGA codon for tryptophan. Reviewed

    Hayashi-Ishimaru, Y, Ehara, M, Inagaki, Y, Ohama, T

    Current Genetics   32 ( 4 )   296-299   1997.10

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  • Algae or protozoa: phylogenetic position of euglenophytes and dinoflagellates as inferred from mitochondrial sequences. Reviewed

    Inagaki, Y, Hayashi-Ishimaru, Y, Ehara, M, Igarashi, I, Ohama, T

    Journal of Molecular Evolution   45 ( 3 )   295-300 - 300   1997.9

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  • Use of a deviant mitochondrial genetic code in yellow-green algae as a landmark for segregating members within the phylum. Reviewed

    Ehara, M, Hayashi-Ishimaru, Y, Inagaki, Y, Ohama, T

    Journal of Molecular Evolution   45 ( 2 )   119-24 - 124   1997.8

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  • 藻類のミトコンドリアに見られる遺伝暗号の変異と藻類の系統

    Plant Morphology   9   51 - 58   1997

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  • UAG is a sense codon in several chlorophycean mitochondria Reviewed

    Y Hayashi-Ishimaru, T Ohama, Y Kawatsu, K Nakamura, S Osawa

    CURRENT GENETICS   30 ( 1 )   29 - 33   1996.6

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    The mitochondrial genetic code of those land plants and green algae that have been examined does not deviate from the universal one. A red alga, Chondrus crispus, is the sole reported example throughout the algae that uses a deviant (non-universal) mitochondrial genetic code (UGA = Trp). We have analyzed 366-bp DNA sequences of the gene for mitochondrial cytochrome oxidase subunit I (COXI) from ten chlorophyceaen algae, and detected 3-8 in-frame UAG codons in the sequences of five species. Comparisons of these sequences with those of other algae and land plants have shown that most of the UAG sites in Hydrodictyon reticulatum, Pediastrum boryanum and Tetraedron bitridens correspond to alanine, and those of Coelastrum microporum and Scenedesmus quadricauda to leucine. The three species in which UAG probably codes for alanine are characterized by zoospore formation in asexual reproduction and form a clade in the COXI phylogenetic tree. The two species in which UAG codes for leucine are known to form daughter coenobia and pair in the tree. This is the first report on a deviant mitochondrial genetic code in green algae. Mutational change(s) in the release factor corresponding to UAG would be involved in these code changes. No genetic code deviation has been found in five other species examined.

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  • Localization of DNA in the condensed interphase chromosomes of Euglena Reviewed

    Katsumi Ueda, Yasuko Hayashi-Ishimaru

    Chromosoma   104   380 - 385   1996

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  • Detection of DNA in the nucleoids of chloroplasts and mitochondria in Euglena gracilis by immunoelectron microscopy. Reviewed

    Yasuko Hayashi-Ishimaru, Katsumi Ueda, Mitsuko Nonaka

    Journal of Cell Science   105   1159 - 1164   1993

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  • Effects of ethidium bromide and chloramphenicol on the mitochondrial nucleoids in Euglena gracilis. Reviewed

    Yasuko Hayashi, Katsumi Ueda

    Physiol. Plant,   86   57 - 62   1992

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  • The shape of mitochondria and the number of mitochondrial nucleoids during the cell cycle of Euglena gracilis. Reviewed

    Yasuko Hayashi, Katsumi Ueda

    Journal of cell Science   93   565 - 570   1989

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  • Localization of mannose, N-acetylglucosamine and galactose in the Golgi apparatus, plasma membranes and cell walls of Scenedesmus acuminatus. Reviewed

    Yasuko Hayashi, Katsumi Ueda

    Plant Cell Physiology   28 ( 8 )   1357 - 1362   1987

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    The localization of lectin binding sites in the Golgi apparatus, plasma membranes and cell walls of Scenedesmus acuminatus was investigated by cytochemical electron microscopy. The lectins used were concanavalin A (Con A), peanut agglutinin (PNA) and wheat germ agglutinin (WGA), all labeled with gold. Con A-gold particles were deposited not on the Golgi apparatus, but on the outer cell-wall layer. PNA-gold and WGA-gold particles were deposited on distal Golgi cisternae and vesicles derived from the Golgi apparatus. Entire cell-wall layers were evenly labeled by PNA-gold. The plasma membrane and cytoplasmic regions close to the plasma membrane were labeled with WGA-gold. The processing of oligosaccharide in the Golgi apparatus, plasma membranes and cell walls of Scenedesmus acuminatus is discussed in reference to that reported for animal cells.

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    Other Link: https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=180561

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  • ATLAS OF PLANT CELL STRUCTURE (HB 2014) [Paperback] [Jan 01, 2014]

    2017  ( ISBN:9784431549406

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  • 超微細構造から紐解くシロイヌナズナの子葉細胞内オルガネラの機能解析

    林 八寿子

    [林八寿子]  2007 

  • 植物の細胞を観る実験プロトコール―顕微鏡観察の基本から最新バイオイメージング技術まで (細胞工学別冊―植物細胞工学シリーズ)

    福田 裕穂, 西村 幹夫, 中野 明彦

    秀潤社  2006.3  ( ISBN:4879622990

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    Total pages:243  

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  • モデル植物の実験プロトコール―イネ・シロイヌナズナ・ミヤコグサ編 (細胞工学別冊―植物細胞工学シリーズ)

    島本 功, 岡田 清孝, 田畑 哲之

    秀潤社  2005.3  ( ISBN:4879622869

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    Total pages:324  

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  • 朝倉植物生理学講座〈1〉植物細胞

    西村 幹夫

    朝倉書店  2002.8  ( ISBN:4254176554

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    Total pages:179  

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  • モデル植物ラボマニュアル―分子遺伝学・分子生物学的実験法 (Springer Lab Manual)

    岩渕 雅樹, 島本 功, 岡田 清孝

    シュプリンガー・フェアラーク東京  2000.4  ( ISBN:4431708812

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MISC

  • Efficient protein transport to peroxisomes requires ubiquitin-conjugating activity by PEX4 in Arabidopsis thaliana

    真野昌二, 真野昌二, 林八寿子, 林八寿子, 曳野和美, 大友政義, 金井雅武, 西村幹夫

    日本分子生物学会年会プログラム・要旨集(Web)   45th   2022

  • Analysis of the mechanism and regulation of protein transport to peroxisomes using Arabidopsis apem mutants

    真野昌二, 真野昌二, 林八寿子, 林八寿子, 曳野和美, 大友政義, 金井雅武, 西村幹夫

    日本植物生理学会年会(Web)   63rd   2022

  • シロイヌナズナATG2変異体におけるPI3PとATG18aの局在解析

    霜田圭祐, 早乙女真穂, 及川和聡, 真野昌二, 西村幹夫, 林八寿子

    Plant Morphology   30 ( 1 )   2018.3

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  • シャジクモの造精糸分裂過程におけるペルオキシソームの挙動解析

    中野渉, 林八寿子

    Plant Morphology   27 ( 1 )   67   2015.4

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  • シロイヌナズナの子葉細胞内における脂質代謝に関する機能形態学的解析

    岡村法子, 林八寿子, 林誠, 真野昌二, CUI Songkui, 西村幹夫

    Plant Morphol   26 ( 1 )   79   2014.4

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  • 高圧凍結および凍結置換法を用いた車軸藻Chara brauniiの精子形成過程の観察

    中野渉, 林八寿子

    藻類   61 ( 1 )   53   2013.3

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  • シャジクモの雄性配偶子形成過程におけるペルオキシソームの挙動解析

    中野渉, 林八寿子

    藻類   60 ( 2 )   118   2012.7

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  • シャジクモの精子形成過程におけるオルガネラの挙動解析―特にペルオキシソームに着目して―

    中野渉, 林八寿子

    Plant Morphol   24 ( 1 )   128   2012.4

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  • イネヌクレオチドピロホスファターゼ/ホスホジエステラーゼのプラスチド局在に関する研究

    梅澤幸歩, 金古堅太郎, 甲州努, 石本卓也, 伊藤紀美子, 林八寿子, 豊岡公徳, 三ツ井敏明

    日本農芸化学会大会講演要旨集(Web)   2012   4A30A10 (WEB ONLY)   2012.3

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  • イネヌクレオチドピロホスファターゼ/ホスホジエステラーゼのプラスチド局在化機構に関する研究

    梅澤幸歩, 金古堅太郎, 甲州努, 石本卓也, 伊藤紀美子, 林八寿子, 豊岡公徳, 三ツ井敏明

    生化学   ROMBUNNO.3P-0301   2011

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  • 緑藻におけるペルオキシソームの単離と機能解析

    野村佳那, 橋詰由美子, 篠崎晃子, 林八寿子

    日本植物学会大会研究発表記録   74th   232   2010.9

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  • シロイヌナズナのペルオキシソーム局在型リンゴ酸脱水素酵素変異体の機能形態学的解析

    林八寿子, 五十嵐健太, 佐藤友博, 加藤朗

    Plant Morphol   22 ( 1 )   87   2010.4

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  • シロイヌナズナ小胞体の形態維持のための新しい分子機構

    中野亮平, 松島良, 上田晴子, 田村謙太郎, 嶋田知生, 李立新, 林八寿子, 近藤真紀, 西村幹夫, 西村いくこ

    日本植物生理学会年会要旨集   51st   133   2010.3

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  • ERMO1/GNOM-LIKE1 and ERMO2/SEC24a Are Required for Maintenance of Endoplasmic Reticulum in Arabidopsis thaliana. Reviewed

    R. T. Nakano, R. Matsushima, H. Ueda, K. Tamura, T. Shimada, L. Li, Y. Hayashi, M. Kondo, M. Nishimura, I. Hara-Nishimura

    21st International Conference on Arabidopsis Research 2010, Yokohama (Japan), June 6-10, 2010   2010

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  • Novel Molecular Pathways Underlying Maintenance of Endoplasmic Reticulum Morphology in <i>Arabidopsis thaliana</i>.

    Nakano Ryohei Thomas, Hara-Nishimura Ikuko, Matsushima Ryo, Ueda Haruko, Tamura Kentaro, Shimada Tomoo, Li Lixin, Hayashi Yasuko, Kondo Maki, Nishimura Mikio

    Plant and Cell Physiology Supplement   2010 ( 0 )   129 - 129   2010

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    The endoplasmic reticulum (ER) forms a dynamic polygonal network composed of tubules, sheets, and three-way junctions. Although the complex ER morphology supports the diverse cellular functions, the molecular mechanisms responsible for the organization of these structures are obscure. Here we report the isolation and characterization of mutants of <i>Arabidopsis thaliana</i> that are defective in ER morphology (<i>ermo1</i>, <i>ermo2</i>, and <i>ermo3</i>). Among three mutants, <i>ermo1</i> and <i>ermo2</i>, which showed partially similar phenotypes, were defective in GNOM-LIKE1 (GNL1) and SEC24a, respectively (1). Both GNL1/ERMO1 and SEC24a/ERMO2 were thought to be involved in the ER-Golgi transport. Our results suggests that the unknown cargo proteins that are specifically transported by GNL1/ERMO1 and SEC24a/ERMO2 may have crucial roles. On the other hand, we identified the responsible gene for <i>ermo3</i> to be a member of GDSL-motif lipase family, which is predicted to be localized within the vacuoles. Our findings suggest a novel pathway that connects ER morphology to lipid metabolic processes.<br>(1) Nakano, R.T. et al., Plant Cell,10.1105/tpc.109.068270 (2009).

    DOI: 10.14841/jspp.2010.0.0129.0

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  • 小胞体の形態と細胞内分布に異常を示すendoplasmic reticulum morphology(ermo)変異体の解析

    中野亮平, 松島良, 上田晴子, 林八寿子, 田村謙太郎, 嶋田知生, 西村いくこ

    日本植物生理学会年会要旨集   50th   117   2009.3

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  • Physiological roles of two malate dehydrogenase isoforms in plant peroxisomes

    Igarashi Kenta, Hayashi Yasuko, Kato Akira

    Supplement   2009 ( 0 )   724 - 724   2009

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    In higher plants, peroxisomes are known to differentiate into several classes. Glyoxysomes that are abundant in cotyledons, contain enzymes of &amp;beta;-oxidation and glyoxylate cycle to degrade storage lipid for postgerminative growth of oilseed plants. Leaf peroxisomes that are found in green leaves, function together with chloroplasts and mitochondria in phororespiration. Malate dehydrogenase (MDH) is an enzyme to catalayze the interconversion of malate and oxaloacetate. Two isoforms of peroxisomal MDH (PMDH) have been identified, the glyoxysome-type isoform, PMDH1 (At2g22780) which is involved in glyoylate cycle and in &amp;beta;-oxidation, and the leaf peroxisome-type isoform, PMDH2 (At5g09660) which is induced by light but those function are not elucidated. We investigated &lt;I&gt;pmdh2&lt;/I&gt; and &lt;I&gt;pmdh1pmdh2&lt;/I&gt; mutants of &lt;I&gt;Arabidopsis&lt;/I&gt; to elucidate physiological function of PMDH2. In this study, we report the phenotypes of these mutants that are grown under high light condition and discuss the function of PMDH2 in leaves.

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  • Analysis of <i>endoplasmic reticulum morphology</i> (<i>ermo</i>) Mutants that Show Defects of ER Morphology and Distribution

    Nakano Ryohei Thomas, Matsushima Ryo, Ueda Haruko, Hayashi Yasuko, Tamura Kentaro, Shimada Tomoo, Hara-Nishimura Ikuko

    Plant and Cell Physiology Supplement   2009 ( 0 )   35 - 35   2009

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    The endoplasmic reticulum (ER) has dynamic structures; i.e., the polygonal network composed of sheets, tubules, and "three-way junctions". To identify the factors responsible for ER morphology, we isolated the mutants that showed defects in ER morphology, and designated them <I>endoplasmic reticulum morphology</I> (<I>ermo</I>). <I>ermo1</I> and <I>ermo2</I> developed a number of ER-derived spherical structures, while <I>ermo3</I> developed a large aggregate within the cells. The spherical structures in <I>ermo2</I> also formed a large aggregate. In <I>ermo1</I> and <I>ermo2</I>, the genes involved in COPI and COPII formation, respectively, were mutated. However, we could not find any defects of membrane trafficking in these mutants, suggesting that ERMO1 and ERMO2 have a novel function in maintaining ER morphology. Alternatively, it is possible that ER-Golgi transport plays a crucial role in ER morphology. In addition, ERMO2 and ERMO3 were shown to be required for keeping organelles distributed throughout the cells.

    DOI: 10.14841/jspp.2009.0.0035.0

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  • Functional Analysis of Peroxisomal Malate Dehydrogenase

    Igarashi Kenta, Sato Yori, Fujiwara Emi, Hayashi Yasuko, Kato Akira

    Supplement   2008 ( 0 )   425 - 425   2008

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    In higher plants, peroxisomes are known to differentiate into several classes. Glyoxysomes that are abundant in cotyledonary cells, contain enzymes of &amp;beta;-oxidation and glyoxylate cycle to degrade storage lipids for postgerminative growth of oil-seed plants. Peroxisomal malate dehydrogenase(PMDH), that is an enzyme of glyoxylate cycle, has two isoforms, At2g22780(PMDH1) and At5g09660(PMDH2). RT-PCR analysis showed that transcription of PMDH1 was activated during germination and that of PMDH2 was induced in response to light. These data suggest that PMDH1 and PMDH2 play different roles, respectively. Therefore, we investigated Arabidopsis &lt;I&gt;pmdh&lt;/I&gt; mutants to elucidate physiological functions of PMDH isoforms. &lt;br&gt;The &lt;I&gt;pmdh1&lt;/I&gt; and &lt;I&gt;pmdh2&lt;/I&gt; display no phenotypic abnormalities during germination. However, &lt;I&gt;pmdh1pmdh2&lt;/I&gt; requires sucrose for postgerminative growth and defects &amp;beta;-oxidation as well as &lt;I&gt;ped1&lt;/I&gt;. These results suggest that PMDHs participate not only in glyoxylate cycle but also in &amp;beta;-oxidation.

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  • 作物の形態研究法 : マクロからミクロまで : 高圧凍結および凍結置換法による電子顕微鏡試料作成

    林 八寿子

    日本作物學會紀事   76 ( 1 )   128 - 130   2007.1

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    電子顕微鏡用の試料作成法としては,簡便な化学固定法が主流であるが,細胞内のより微細な構造の解析や,瞬間的な動きを捉えるため,また,免疫電子顕微鏡法のための抗原性の保持のためには,凍結固定法が優れている.近年,高圧下で凍結することで,構造を破壊する原因である氷結の形成を防ぐことができる高圧凍結装置(Bal-Tec, HPM010S型)が開発され,組織を材料とした凍結固定法による試料作成が可能となっている.そこで,この装置を用いた高圧凍結および凍結置換法について紹介する.

    DOI: 10.1626/jcs.76.128

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  • 作物の形態研究法:マクロからミクロまで 高圧凍結および凍結置換法による電子顕微鏡試料作成

    林 八寿子

    日作紀   76 ( 1 )   128 - 130   2007

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    電子顕微鏡用の試料作成法としては,簡便な化学固定法が主流であるが,細胞内のより微細な構造の解析や,瞬間的な動きを捉えるため,また,免疫電子顕微鏡法のための抗原性の保持のためには,凍結固定法が優れている.近年,高圧下で凍結することで,構造を破壊する原因である氷結の形成を防ぐことができる高圧凍結装置(Bal-Tec, HPM010S型)が開発され,組織を材料とした凍結固定法による試料作成が可能となっている.そこで,この装置を用いた高圧凍結および凍結置換法について紹介する.

    DOI: 10.1626/jcs.76.128

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  • シロイヌナズナAtVAM3(SNAREタンパク質VAM3ホモログ)はミロシン細胞の分化に関与する

    上田晴子, 西山千晶, 嶋田知生, 河本恭子, 林八寿子, 近藤真紀, 大友一郎, 高橋卓, 西村幹夫, 西村いくこ

    日本植物生理学会年会要旨集   47th   196   2006.3

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  • AtVAM3, a homolog of Q(a)-SNARE VAM3, is involved in development of rnyrosin cells in Arabidopsis

    H Ueda, C Nishiyama, T Shimada, Y Koumoto, Y Hayashi, M Kondo, Ohtomo, I, T Takahashi, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   47 ( 0 )   S116 - S116   2006

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:OXFORD UNIV PRESS  

    Yeast VAM3 is a Q&lt;SUB&gt;a&lt;/SUB&gt;-SNARE that is involved in vacuolar transport of proteins and vacuolar assembly. Previously, we showed that &lt;I&gt;atvam3&lt;/I&gt; mutants accumulate large amounts of thioglucoside glucohydrolase (TGG), which hydrolyze glucosinolates to produce toxic compounds for repelling pests. Myrosin cells in &lt;I&gt;Capparales&lt;/I&gt; plants are idioblasts that accumulate TGG. An immunogold revealed TGGs were specifically localized in the vacuole of myrosin cells in &lt;I&gt;atvam3&lt;/I&gt; mutants. This result indicates that TGGs are normally transported to vacuoles in these mutants and that AtVAM3 is not essential for vacuolar transport of TGG. Myrosin cells were scattered along leaf veins in wild-type leaves, while they were abnormally distributed in &lt;I&gt;atvam3&lt;/I&gt; leaves. The mutants developed a network of myrosin cells throughout the leaves: myrosin cells were not only distributed continuously along leaf veins, but were also observed independent of leaf veins. Our results suggest that AtVAM3 has a plant-specific function in development of myrosin cells.

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  • シロイヌナズナの異型細胞(ミロシン細胞)分化にはSNAREタンパク質AtVAM3が関与する

    上田晴子, 西山千晶, 嶋田知生, 河本恭子, 林八寿子, 大友一郎, 高橋卓, 西村いくこ

    日本分子生物学会年会講演要旨集   28th   722   2005.11

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  • Reporter gene assay of targeting signal-like elements and the expression pattern of peroxisomal enzymes in Chlamydomonas reinhardtii

    A Shinozaki, N Sato, Y Hayashi

    PLANT AND CELL PHYSIOLOGY   46 ( 0 )   S230 - S230   2005

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    Peroxisome is an organelle that exists universally in eukaryotic cells, however the function of it differs among species and type of tissues. In higher plants, peroxisomes are directly transformed from glyoxysomes to leaf peroxisomes in greening cotyledons of fatty seedlings. Glyoxisomes contain enzymes for the fatty acid &amp;beta;-oxidation cycle and the glyoxylate cycle, while leaf peroxisomes contain enzymes for photorespiration pathway. Reverse transformation of leaf peroxisomes to glyoxysomes is observed in the senescing cotyledons. Almost of peroxisomal enzymes bear an element that works as a peroxisomal targeting signal (PTS). We detected a PTS1-like element in malate synthase and glycolate oxidase genes of&lt;I&gt;Chlamydomonas reinhardtii&lt;/I&gt;. To know these enzymes are actually located in the peroxisomes and if higher plant&#039;s PTS acts normally in this unicellular green alga, we expressed a fusion gene of GFP with PTS. We also analyzed expression patterns of these enzymes in photoautotrophic and heterotrophic growth conditions.

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  • Morphological analysis of ER body mutants in Arabidopsis

    T Sakurai, R Matsushima, Y Hayashi, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   46 ( 0 )   S154 - S154   2005

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    ER body is a compartment that is derived from endoplasmic reticulum in &lt;I&gt;Arabidopsis thaliana&lt;/I&gt;. They are distributed in the epidermal cells of whole seedlings, while rosset leaves have no ER bodies. However, ER bodies are induced in rosset leaves by wounded stress and/or treatment with methyl jasmonate. This indicates that the ER body plays a role in the defense system of plants (Matsushima et al.,2003). Fluorescent ER bodies were observed in transgenic plants of Arabidopsis expressing GFP fused with an ER retention signal (&lt;I&gt;GFP-h&lt;/I&gt;). To know the mechanism of ER body formation, we raised several kinds of morphological ER body mutants by EMS treatment of the epidermal cells of cotyledons from &lt;I&gt;GFP-h&lt;/I&gt; seeds. We will report the morphological features of these mutants obtained through observations by conforcal laser scan microscope and transmission electron microscope. Based on these, we would like to discuss the mechanism of the formation of ER bodies.

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  • Analysis of the Arabidopsis mutant accumulating a large amount of myrosinases

    H Ueda, C Nishiyama, J Nakamura, Y Hayashi, Ohtomo, I, T Takahashi, T Shimada, Nishimura, I

    PLANT AND CELL PHYSIOLOGY   46 ( 0 )   S153 - S153   2005

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:OXFORD UNIV PRESS  

    Myrosinases are &amp;beta;-glucosidases that are found mainly in the order Capparales. Myrosinases hydrolyze glucosinolates to produce the toxic compounds for the pests. The abnormal accumulation of myrosinases was found in &lt;I&gt;Arabidopsis&lt;/I&gt; mutants of AtVAM3, which is a syntaxin homolog to yeast VAM3 involved in the vacuolar assembly. In this study, we characterized the abnormal accumulation of myrosinases in two AtVAM3 mutants; one expresses the insertion form of AtVAM3 with an additional peptide and another is a knockout mutant of the &lt;I&gt;AtVAM3&lt;/I&gt; gene. The organ specific expression and the localization to the myrosin cells of the myrosinases in these mutants were the same as in wild-type. Interestingly, the numbers of the myrosin cells were markedly increased in the mutants. The abnormal accumulation of myrosinases in the mutants might be caused by the excessive occurrence of the myrosin cells. These results suggest that AtVAM3 is involved in differentiation of myrosin cells.

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  • Analysis of differentiation of endoplasmic reticulum with green/red fluorescent proteins

    H Ueda, Y Hayashi, T Shimada, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   45   S209 - S209   2004

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  • 蛍光タンパク質を用いた小胞体の分化の解析

    上田晴子, 林八寿子, 嶋田知生, 西村いくこ

    日本植物生理学会年会要旨集   45th   2004

  • High Pressure Freezing for Plant Cells

    HAYASHI Yasuko

    Electron-microscopy   37   121 - 124   2002.11

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  • シロイヌナズナの表皮細胞に局在する小胞体由来の新規構造体(ER body)の解析

    松島良, 林八寿子, 山田健志, 嶋田知生, 西村幹夫, 西村いくこ

    日本植物生理学会年会要旨集   42nd   228   2002.3

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  • The analysis of the ER-derived organelles localized in the epidermal cells of Arabidopsis

    R Matsushima, Y Hayashi, K Yamada, T Shimada, M Nishimura, Hara-Nishimura, I

    PLANT AND CELL PHYSIOLOGY   43   S188 - S188   2002

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  • 子葉の老化で消失するシロイヌナズナの表皮細胞に見られるER由来の新規構造体の解析

    石丸八寿子, 山田健志, 松島良, 嶋田知生, 西沢直子, 西村いくこ, 西村幹夫

    日本植物生理学会年会要旨集   41st   2001

  • 液胞輸送レセプターPV72の細胞内局在性と役割

    嶋田知生, 三橋尚登, 石丸八寿子, 西村幹夫, 西村いくこ

    日本植物生理学会年会要旨集   41st   2001

  • Comprehensive molecular phylogenetic analysis of a heterokont alga (NIES 548) using genes from all three cellular compartments

    Megumi Ehara, Taiju Kitayama, Kazuo I. Watanabe, Yuji Inagaki, Yasuko Hayashi-Ishimaru, Takeshi Ohama

    Phycological Research   47 ( 3 )   225 - 231   1999

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    We have determined a partial DNA sequence (approximately 1.1 kb) encoding the mitochondrial cytochrome oxidase subunit 1 (cox1) gene from the alga NIES 548, a strain which has been maintained as Tribonema marinum J. Feldmann (Xanthophyceae) at the National Institute of Environmental Study (NIES, Japan). Unexpectedly, phylogenetic analysis of cox1 sequences showed that NIES 548 does not group with Xanthophyceae, but groups strongly with the Phaeophyceae. Furthermore, the cox1 sequence from NIES 548 does not use the codon AUA for methionine (AUA/Met), a genetic marker characteristic for the Xanthophyceae. Given the cox1 results, the molecular phylogenetic position of NIES 548 was thus examined with DNA sequences from genes encoded in the two other subcellular compartments. In the plastid, we analyzed elongation factor tu (tufA) and in the nucleus, the small subunit ribosomal RNA (rrnS). These analyses clearly indicated that NIES 548 is not a member of the Xanthophyceae, but a member of the Phaeophyceae. This result is robust as it was supported by all three genes analyzed, each of which reside in different genomes. The phylogenetic resolutions of these trees were almost the same, proving the usefulness of mitochondrial cox1 gene as a tool for phylogenetic reconstruction in the phycological arena. Our light microscopic observations indicated that NIES 548 is a uniseriate filamentous alga with branches, a clear contradiction of its original descriptions. We conclude that NIES 548 is a phaeophycean alga and is not the same clone of the strain observed by Sartoni and his co-authors.

    DOI: 10.1046/j.1440-1835.1999.00166.x

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  • ミトコンドリア遺伝子による藻類の分子系統としての遺伝暗号変異 (その1)

    江原 恵, 石丸 八寿子, 稲垣 祐司, 大濱 武

    日本植物学会大会研究発表記録 = Proceedings of the annual meeting of the Botanical Society of Japan   61   255 - 255   1997.9

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  • 藻類, 原生植物, ミトコンドリアの遺伝暗号変異の方向性 (その2)

    大濱 武, 稲垣 祐司, 江原 恵, 石丸 八寿子

    日本植物学会大会研究発表記録 = Proceedings of the annual meeting of the Botanical Society of Japan   61   255 - 255   1997.9

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  • ミトコンドリア遺伝子による藻類の分子系統解析 黄色植物の分子系統と遺伝暗号変異

    江原 恵, 稲垣 祐司, 石丸 八寿子, 大浜 武

    藻類   45 ( 1 )   70 - 70   1997.3

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  • COXI 遺伝子による渦鞭毛藻類の系統解析

    稲垣 祐司, 江原 恵, 石丸 八寿子, 大浜 武

    藻類   45 ( 1 )   70 - 70   1997.3

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  • カサノリ目 Acetabularia calyculus のミトコンドリア遺伝子 COXl の遺伝暗号変異

    江原 恵, 稲垣 祐司, 石丸 八寿子, 大濱 武

    藻類   45 ( 1 )   78 - 78   1997.3

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  • 藻類における分子マーカーとしてのミトコンドリア遺伝暗号変異

    石丸 八寿子, 田中 嗣子, 大浜 武

    藻類   44 ( 1 )   60 - 60   1996.3

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  • 藻類のミトコンドリアCOXIにおける遺伝暗号の変化と分子系統

    石丸 八寿子, 河津 実良, 大濱 武

    日本植物学会大会研究発表記録 = Proceedings of the annual meeting of the Botanical Society of Japan   59   199 - 199   1995.9

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  • 緑藻ミトコンドリアCOXI遺伝子に見いだされた遺伝暗号変異と分子系統樹

    石丸 八寿子, 大浜 武

    藻類   43 ( 1 )   88 - 88   1995.3

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  • ミトコンドリアCOXI遺伝子によるEuglenaの系統的位置とその葉緑体起源の推定

    石丸 八寿子, 大浜 武

    藻類   43 ( 1 )   88 - 88   1995.3

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Awards

  • 日本植物生理学会論文賞

    2003.3   日本植物生理学会  

    林八寿子, 松島良, 西村いくこ, 西村幹夫, 西澤直子, 嶋田知生, 山田健志

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    Award type:Honored in official journal of a scientific society, scientific journal  Country:Japan

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  • 日本植物形態学会奨励賞

    1997.9   日本植物形態学会  

    石丸(林)八寿子

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    Award type:International academic award (Japan or overseas)  Country:Japan

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Research Projects

  • Mechanism of lipid body degradation drived by light in cotyledon cells

    Grant number:22K06292

    2022.4 - 2026.3

    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

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

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  • 林木初のピラミッディング育種技術の高度化と実用化に向けた検証

    Grant number:21K05666

    2021.4 - 2026.3

    System name:科学研究費助成事業 基盤研究(C)

    Research category:基盤研究(C)

    Awarding organization:日本学術振興会

    森口 喜成, 林 八寿子, 岩井 淳治

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    Grant amount:\4030000 ( Direct Cost: \3100000 、 Indirect Cost:\930000 )

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  • Analyses of abnormal physiological responses induced by stable resin nanoparticles and its species spectrum

    Grant number:19K12422

    2019.4 - 2022.3

    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

    Ohama Takeshi

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

    Isobutylcyanoacrylate nano particle (iBCA-NP), ethyl particles (ECA-NP), methyl particles (MCA-NP), and isopropyl particles (iPCA-NP) were prepared using Tween 80. The growth inhibitory potential of these particles was tested using bacteria, yeasts, and green algae. iBCA-NPs often showed the weakest cell growth inhibitory potential, and ECA-NPs showed the greatest cell death inducing potential against the greatest tested species. iPCA-NPs were effective in several green algae, where iBCA-NPs and ECA-NPs' exposure had no effect on growth at all.
    In some cases, the effects of nanoparticle exposure were quite different even among closely related species.

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  • Analysis of the mechanism of regulation of the disappearance of excess lipid body in plant cells.

    Grant number:17K07467

    2017.4 - 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

    HAYASHI YASUKO

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

    In the cotyledonary cells of Arabidopsis, peroxisomes come into contact with lipid bodies and produce the necessary energy after germination. However, the presence of sucrose in the medium reduces this contact and does not reduce storage lipids. At this time, it was suggested that the endoplasmic reticulum may regulate the metabolic rate of peroxisomes by surrounding the lipid body. It was also shown that the excess storage lipids that became unnecessary due to the greening of cotyledons is reduced not only by the metabolism of peroxisomes but also by other disappearance mechanisms. In addition, it was shown that the lipid bodies accumulated in unicellular green algae cells of Chlamydomonas due to nitrogen deficiency may be degraded by a mechanism such as autophagy rather than the peroxisome metabolism system.

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  • Analysis of plastid-targeting mechanism of glycoproteins involved in starch metabolism of rice

    Grant number:22380186

    2010.4 - 2014.3

    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

    MITSUI Toshiaki, ITOH Kimiko, HAYASHI Yasuko, HANASHIRO Isao, OHTSUBO Ken-ichi

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    Grant amount:\18200000 ( Direct Cost: \14000000 、 Indirect Cost:\4200000 )

    (1) We found that rice AmyI-1, NPP1, NPP2, NPP6, and MSD1 are glycoproteins targeting to plastid via the secretory pathway, and we characterized N-glycome (oligosaccharide structures) of plastidial glycoprotein NPP1. (2) The plastid targeting signal regions (PT) of AmyI-1 and NPP1 were identified. Furthermore, it was suggested that there exists plastid envelope factor(s) that required for plastid targeting of glycoprotein. (3) Abnormal expression of alpha-amylase during seed development led to the poor formation of starch granule. In addition, NPP1 was found to be a negative regulator for starch accumulation in rice leaves.

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  • Functional analysis of organelle in the cotyledonous cells of Arabidopsis thaliana under the ultrastructural research.

    Grant number:15570048

    2003 - 2006

    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

    HAYASHI Yasuko

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    Grant amount:\3700000 ( Direct Cost: \3700000 )

    We have interested in the mechanism of organelle and the transport between organelle. To examine the formation mechanism of ER body that existed in the peculiarity in epidermal cell of the nourishment organ such as cotyledon of Arabidopsis thaliana, the ER-body form mutant was analyzed. Our data from ultra-microscopic analysis and immune-electron microscopic analysis revealed that the formation of ER-body was obstructed in A2 mutant line, and GFP-HDEL synthesized by the rough endoplasmic reticulum was not discharged from the endoplasmic reticulum lumen. As a result, GFP-HDEL had accumulated abnormally in the endoplasmic reticulum lumen. In A28 and the B23 mutant lines, GFP-HDEL did not stay in the endoplasmic reticulum lumen and was discharged from endoplasmic reticulum. As a result, GFP-HDEL had being packed into the follicle structure formed differing from ER body abnormally. It was guessed that three genes or more took part from this for a normal formation and the function of ER body. From the rough mapping of the cause gene about A28 line, we identified the candidate gene existed in the vicinity of the YUP4G12RE marker on the third chromosome. From the analysis of two syntaxin (Vam3) mutants that abnormality accumulated myrosinases, we found that the myrosin cell had been accumulated voluminously in vacuole and ER-body-like structure took part in the accumulation process. It was suggested that ER-body carry out various functions by the difference of the tissues.
    In addition to these, we examined whether rapid frozen metal contact device (HIF-4K) was able to be used for the frozen fixation of the plant organization cell, and it was confirmed that both success rates and the qualities of pressurizing frozen device (HPM-010) were more effective than HIF-4K device.

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Teaching Experience

  • 自然環境科学研究演習

    2023
    Institution name:新潟大学

  • 環境経済システム論I

    2022
    Institution name:新潟大学

  • 理学基礎演習

    2022
    Institution name:新潟大学

  • 自然科学基礎実験

    2022
    Institution name:新潟大学

  • 安全教育

    2022
    Institution name:新潟大学

  • 生物学実験

    2022
    Institution name:新潟大学

  • 古環境学

    2021
    Institution name:新潟大学

  • 機能形態学特論

    2021
    Institution name:新潟大学

  • 自然環境科学特論C

    2021
    Institution name:新潟大学

  • 課題研究B

    2021
    Institution name:新潟大学

  • 課題研究C

    2021
    Institution name:新潟大学

  • 自然環境科学実験B2

    2020
    Institution name:新潟大学

  • 生物学基礎実習a

    2020
    Institution name:新潟大学

  • 課題研究(自然環境)B

    2020
    Institution name:新潟大学

  • 課題研究

    2020
    -
    2021
    Institution name:新潟大学

  • 自然環境科学実験B1

    2018
    Institution name:新潟大学

  • 自然環境科学総論

    2018
    Institution name:新潟大学

  • 理学スタディ・スキルズ

    2018
    -
    2021
    Institution name:新潟大学

  • 生物学基礎実習b

    2018
    Institution name:新潟大学

  • 課題研究B

    2017
    -
    2021
    Institution name:新潟大学

  • 課題研究C

    2017
    -
    2021
    Institution name:新潟大学

  • 課題研究A

    2017
    -
    2021
    Institution name:新潟大学

  • 専門力アクティブ・ラーニング

    2017
    -
    2018
    Institution name:新潟大学

  • 自然科学基礎実験

    2017
    Institution name:新潟大学

  • 生物形態機能論

    2016
    Institution name:新潟大学

  • 多様性生物学A

    2015
    -
    2018
    Institution name:新潟大学

  • 課題研究(自然環境)

    2015
    Institution name:新潟大学

  • 自然科学実験法

    2014
    -
    2017
    Institution name:新潟大学

  • 環境科学スタディスキルズ

    2014
    -
    2016
    Institution name:新潟大学

  • 環境経済システム論I

    2014
    -
    2015
    Institution name:新潟大学

  • 環境科学演習Ⅰ

    2014
    Institution name:新潟大学

  • 環境科学特定研究

    2014
    Institution name:新潟大学

  • 中間発表D

    2014
    Institution name:新潟大学

  • Earth System Science

    2014
    Institution name:新潟大学

  • 生物学-生物多様性A-

    2012
    -
    2013
    Institution name:新潟大学

  • 環境科学総合演習Ⅰ

    2012
    Institution name:新潟大学

  • 環境科学特定研究Ⅰ

    2012
    Institution name:新潟大学

  • 研究者の仕事と生活

    2012
    Institution name:新潟大学

  • 環境科学セミナーⅠ

    2012
    Institution name:新潟大学

  • 適応生物学

    2011
    Institution name:新潟大学

  • 環境生物学野外実習A

    2011
    -
    2013
    Institution name:新潟大学

  • 生物学-生態A-

    2011
    Institution name:新潟大学

  • 生物学-細胞・分子B-

    2009
    -
    2010
    Institution name:新潟大学

  • 環境学入門

    2008
    Institution name:新潟大学

  • 生物学実験 I

    2008
    -
    2017
    Institution name:新潟大学

  • 機能形態学特論Ⅱ

    2008
    -
    2014
    Institution name:新潟大学

  • 生物圏の構造と多様性

    2008
    -
    2010
    Institution name:新潟大学

  • 環境生物学演習

    2007
    Institution name:新潟大学

  • 生物学基礎A

    2007
    Institution name:新潟大学

  • 機能形態学A

    2007
    Institution name:新潟大学

  • 安全教育

    2007
    -
    2022
    Institution name:新潟大学

  • 自然環境科学実験B

    2007
    -
    2018
    Institution name:新潟大学

  • 自然環境科学概論B

    2007
    -
    2016
    Institution name:新潟大学

  • 基礎生物学実験

    2007
    -
    2016
    Institution name:新潟大学

  • 生物形態機能論II

    2007
    -
    2015
    Institution name:新潟大学

  • 生物学-細胞・分子B-

    2007
    -
    2008
    Institution name:新潟大学

  • 日本事情自然系A

    2007
    Institution name:新潟大学

  • 機能形態学特論II

    2007
    Institution name:新潟大学

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