Updated on 2024/05/28

写真a

 
MATSUSHIMA Ryo
 
Organization
Institute of Plant Science and Resources Associate Professor
Position
Associate Professor
External link

Degree

  • 理学 ( 京都大学 )

Research Interests

  • 澱粉

  • オオムギ

  • 胚乳

  • 育種

  • アミロペクチン

  • イネ

Research Areas

  • Environmental Science/Agriculture Science / Science in plant genetics and breeding  / 澱粉科学、穀類、イネ、オオムギ、胚乳

Education

  • Kyoto University    

    1998.4 - 2003.3

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  • 東京大学農学部生物・環境工学専攻 生物システム工学専修    

    1994.4 - 1998.3

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Research History

  • Akita Prefectural University

    2022.4

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  • Okayama University   Institute of Plant Science and Resources   Associate Professor

    2016.4

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  • Okayama University   Institute of Plant Science and Resources

    2011.4 - 2016.3

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  • Okayama University   Institute of Plant Science and Resources   Assistant Professor

    2007.4 - 2011.3

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  • Okayama University   Institute of Plant Science and Resources   Research Assistant

    2005.4 - 2007.3

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  • Kyoto University   Center for Ecological Research

    2004.4 - 2005.3

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  • 京都大学大学院理学研究科   日本学術振興会特別研究員 (PD)

    2003.4 - 2004.3

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  • 京都大学大学院理学研究科   日本学術振興会特別研究員 (DC2)

    2002.4 - 2003.3

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Committee Memberships

  •   倉敷キャンパスマネージメント委員会  

    2024.4   

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  •   組換えDNA実験安全管理委員会  

    2022.4   

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  •   共通機器委員会  

    2022.4   

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  •   組換えDNA実験安全管理委員会 申請・審査の新Webシステムのワーキンググループ  

    2022.4 - 2023.3   

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  •   組換えDNA実験安全主任者 (倉敷地区)  

    2021.4   

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  •   図書委員会  

    2020   

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  •   学術交流委員会 (科学教育研究担当)  

    2020   

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  •   組換えDNA実験安全管理委員会  

    2020   

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  •   地球温暖化対策委員会  

    2020   

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Papers

  • Responses of the marine filamentous red alga ‘Bangia’ sp. ESS1 to recurrent changes in seawater concentration Reviewed

    Kumari, P, Matsushima, R, Hirayama, T, Mikami K

    Algal Research   80   103551   2024.5

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    DOI: 10.1016/j.algal.2024.103551

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  • FLOURY ENDOSPERM 6 mutations enhance the sugary phenotype caused by the loss of ISOAMYLASE1 in barley Reviewed International journal

    Matsushima R*, Hisano H, Galis I, Miura S, Crofts N, Takenaka Y, Oitome NF, Ishimizu T, Fujita N, Sato K

    Theoretical and Applied Genetics   136   94   2023.4

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

    DOI: 10.1007/s00122-023-04339-5

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  • Starch biosynthetic protein complex formation in rice ss2a be2b (+) double mutant differs from their parental single mutants. Reviewed

    Ida T, Crofts N, Miura S, Matsushima R, Fujita N

    Journal of Applied Glycoscience   69 ( 2 )   23 - 22   2022.3

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    Amylopectin, which consists of highly branched glucose polymers, is a major component of starch. Biochemical processes that regulate the elongation of glucose polymers and the generation and removal of glucose branches are essential for determining the properties of starch. Starch synthases (SSs) and branching enzyme (BE) mainly form complexes consisting of SSI, SSIIa, and BEIIb during endosperm development. Loss of BEIIb in rice is complemented by BEIIa, but the compensatory effects differ depending on the presence or absence of inactive BEIIb. To better understand these compensatory mechanisms, ss2a be2b (+) double mutant, which possessed truncated inactive SSIIa and inactive BEIIb, were analyzed. Soluble proteins separated by gel filtration chromatography showed that SSIIa and BEIIb proteins in the wild-type exhibited a broad range of elution patterns and only small amounts were detected in high molecular mass fractions. In contrast, most of truncated inactive SSIIa and inactive BEIIb from ss2a be2b (+) were found in high molecular mass fractions, and the SSI-SSIIa-BEIIb trimeric protein complex found in the wild-type was likely absent in ss2a be2b (+). Those SSIIa and BEIIb proteins in high molecular mass fractions in ss2a be2b (+) were also identified by mass spectrometry. Parental ss2a single mutant had negligible amounts of SSIIa suggesting that the truncated inactive SSIIa was recruited to high-molecular mass complexes in the presence of inactive BEIIb in ss2a be2b (+) double mutant. In addition, SSIVb might be involved in the formation of alternative protein complexes with < 300 kDa in ss2a be2b (+).

    DOI: 10.5458/jag.jag.JAG-2021_0015

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  • Mutation in BEIIb mitigates the negative effect of the mutation in ISA1 on grain filling and amyloplast formation in rice Reviewed

    Nagamatsu S., Wada T., Matsushima R., Fujita N., Miura S., Crofts N., Hosaka Y., Yamaguchi O., Kumamaru T.

    Plant Molecular Biology   108   497 - 512   2022.1

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  • Structure and Properties of Starch in Rice Double Mutants Lacking Starch Synthase (SS) IIa and Starch Branching Enzyme (BE) IIb Reviewed

    Ida T, Crofts N, Miura S, Matsushima R, Fujita N

    Journal of Applied Glycoscience   68 ( 2 )   31 - 39   2021

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    Starch biosynthetic enzymes form multi-protein complexes consisting of starch synthase (SS) I, SSIIa, and starch branching enzyme (BE) IIb, which synthesize amylopectin clusters. This study analyzed the starch properties in two double mutant rice lines lacking SSIIa and BEIIb, one of which expressed an inactive BEIIb protein. The ss2a be2b lines showed similar or greater seed weight than the be2b lines, and plant growth was not affected. The ss2a line showed increased short amylopectin chains resulting in a lower gelatinization temperature. Starch granule morphology and A-type crystallinity were similar between the ss2a line and the wild type, except for a mild chalky seed phenotype in the ss2a line. However, the starch phenotype of the ss2a be2b lines, which was similar to that of be2b but not ss2a, was characterized by increased long amylopectin chains, abnormal starch granules, and B-type crystallinity. The similarity in phenotype between the ss2a be2b and be2b lines may be attributed to the inability of the be2b mutants to generate short amylopectin branches, which serve as primers for SSIIa. Therefore, the presence or absence of SSIIa hardly affected the amylopectin structure under the be2b background. The amylose content was significantly higher in the ss2a be2b lines than in the be2b lines. Starch crystallinity was greater in ss2a be2b lines than in be2b lines, despite the fact that starch crystallinity is generally negatively correlated with amylose content. This suggests that the formation of a double helix between long amylopectin chains and amylose affects starch crystallinity in the ss2a be2b mutants.

    DOI: 10.5458/jag.jag.JAG-2021_0002

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  • Starch biosynthetic protein complex formation in rice ss2a be2b (+) double mutant differs from their parental single mutants Reviewed

    Ida T, Crofts N, Miura S, Matsushima R, Fujita N

    Journal of Applied Glycoscience   69   23 - 33   2021

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  • Imaging Amyloplasts in the Developing Endosperm of Barley and Rice. Reviewed

    Matsushima R*, Hisano H*

    Scientific Reports   9   3745   2019

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  • Rice Mutants Lacking Starch Synthase I or Branching Enzyme IIb Activity Altered Starch Biosynthetic Protein Complexes. Reviewed International journal

    Crofts N, Iizuka Y, Abe N, Miura S, Kikuchi K, Matsushima R, Fujita N

    Frontiers in plant science   9   1817 - 1817   2018

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    Amylopectin, the major component of starch, is synthesized by synergistic activity of multiple isozymes of starch synthases (SSs) and branching enzymes (BEs). The frequency and length of amylopectin branches determine the functionality of starch. In the rice endosperm, BEIIb generates short side chains of amylopectin and SSI elongates those branches, which can be further elongated by SSIIa. Absence of these enzymes greatly affects amylopectin structure. SSI, SSIIa, and BEIIb associate with each other and with other starch biosynthetic enzymes although SSIIa is low activity in japonica rice. The aim of the current study was to understand how the activity of starch biosynthetic enzyme complexes is compensated in the absence of SSI or BEIIb, and whether the compensatory effects are different in the absence of BEIIb or in the presence of inactive BEIIb. Interactions between starch biosynthetic enzymes were analyzed using one ss1 null mutant and two be2b japonica rice mutants (a mutant producing inactive BEIIb and a mutant that did not produce BEIIb). Soluble proteins extracted from the developing rice seeds were separated by gel filtration chromatography. In the absence of BEIIb activity, BEIIa was eluted in a broad molecular weight range (60-700 kDa). BEIIa in the wild-type was eluted with a mass below 300 kDa. Further, majority of inactive BEIIb co-eluted with SSI, SSIIa, and BEI, in a mass fraction over 700 kDa, whereas only small amounts of these isozymes were found in the wild-type. Compared with the be2b lines, the ss1 mutant showed subtle differences in protein profiles, but the amounts of SSIIa, SSIVb, and BEI in the over-700-kDa fraction were elevated. Immunoprecipitation revealed reduced association of SSIIa and BEIIb in the ss1 mutant, while the association of BEIIb with SSI, SSIIa, SSIVb, BEI, and BEIIa were more pronounced in the be2b mutant that produced inactive BEIIb enzyme. Mass spectrometry and western blotting revealed that SSI, SSIIa, SSIIIa, BEI, BEIIa, starch phosphorylase 1, and pullulanase were bound to the starch granules in the be2b mutants, but not in the wild-type and ss1 mutant. These results will aid the understanding of the mechanism of amylopectin biosynthesis.

    DOI: 10.3389/fpls.2018.01817

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  • Deficiency of Starch Synthase IIIa and IVb Alters Starch Granule Morphology from Polyhedral to Spherical in Rice Endosperm Reviewed

    Toyosawa Y, Kawagoe Y, Matsushima R, Crofts N, Ogawa M, Fukuda M, Kumamaru T, Okazaki Y, Kusano M, Saito K, Toyooka K, Sato M, Ai Y, Jane J-L, Nakamura Y, Fujita N

    Plant Physiology   170 ( 3 )   1255 - 1270   2016.3

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    Starch granule morphology differs markedly among plant species. However, the mechanisms controlling starch granule morphology have not been elucidated. Rice (Oryza sativa) endosperm produces characteristic compound-type granules containing dozens of polyhedral starch granules within an amyloplast. Some other cereal species produce simple-type granules, in which only one starch granule is present per amyloplast. A double mutant rice deficient in the starch synthase (SS) genes SSIIIa and SSIVb (ss3a ss4b) produced spherical starch granules, whereas the parental single mutants produced polyhedral starch granules similar to the wild type. The ss3a ss4b amyloplasts contained compound-type starch granules during early developmental stages, and spherical granules were separated from each other during subsequent amyloplast development and seed dehydration. Analysis of glucan chain length distribution identified overlapping roles for SSIIIa and SSIVb in amylopectin chain synthesis, with a degree of polymerization of 42 or greater. Confocal fluorescence microscopy and immunoelectron microscopy of wild-type developing rice seeds revealed that the majority of SSIVb was localized between starch granules. Therefore, we propose that SSIIIa and SSIVb have crucial roles in determining starch granule morphology and in maintaining the amyloplast envelope structure. We present a model of spherical starch granule production.

    DOI: 10.1104/pp.15.01232

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  • Amyloplast Membrane Protein SUBSTANDARD STARCH GRAIN6 Controls Starch Grain Size in Rice Endosperm Reviewed

    Matsushima R*, Maekawa M, Kusano M, Tomita K, Kondo H, Nishimura H, Crofts N, Fujita N, Sakamoto W

    Plant Physiology   170 ( 3 )   1445 - 1459   2016.3

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    Starch is a biologically and commercially important polymer of glucose. Starch is organized into starch grains (SGs) inside amyloplasts. The SG size differs depending on the plant species and is one of the most important factors for industrial applications of starch. There is limited information on genetic factors regulating SG sizes. In this study, we report the rice (Oryza sativa) mutant substandard starch grain6 (ssg6), which develops enlarged SGs in endosperm. Enlarged SGs are observed starting at 3 d after flowering. During endosperm development, a number of smaller SGs appear and coexist with enlarged SGs in the same cells. The ssg6 mutation also affects SG morphologies in pollen. The SSG6 gene was identified by map-based cloning and microarray analysis. SSG6 encodes a protein homologous to aminotransferase. SSG6 differs from other rice homologs in that it has a transmembrane domain. SSG6-green fluorescent protein is localized in the amyloplast membrane surrounding SGs in rice endosperm, pollen, and pericarp. The results of this study suggest that SSG6 is a novel protein that controls SG size. SSG6 will be a useful molecular tool for future starch breeding and applications.

    DOI: 10.1104/pp.15.01811

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  • Geometrical Formation of Compound Starch Grains in Rice Implements Voronoi Diagram Reviewed

    Matsushima R*, Maekawa M, Sakamoto W

    Plant and Cell Physiology   56 ( 11 )   2150 - 2157   2015.11

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:OXFORD UNIV PRESS  

    Starch forms transparent grains, called starch grains (SGs), in amyloplasts. One of the major morphological SG forms in Poaceae, called a compound SG, is formed by assemblies of small starch granules in an amyloplast. Starch granules assemble as a well-ordered structure; however, the mechanism that regulates this organization has not been identified. In this study, we examined how starch granules grow and converge into the final SG morphology. First, we found that the number of starch granules in an amyloplast is almost constant from the early developmental stage until endosperm maturity. Next, we quantitatively evaluated the geometrical similarities between starch granules and a Voronoi diagram, which is a mathematical tessellation of space based on the distance to a specific set of points in the space. The in silico growth simulation showed that the geometrical patterns of compound SGs resembling a Voronoi diagram is determined by physical interactions among the free-growing starch granules and the amyloplast envelope membrane. The geometrical similarity between compound SGs and a Voronoi diagram is likely a result of maximum loading and storage of starch in the amyloplast. The simulation described in this study provides a greater understanding of how compound SGs are formed and also has the potential to explain morphological variations of SGs.

    DOI: 10.1093/pcp/pcv123

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  • Amylopectin biosynthetic enzymes from developing rice seed form enzymatically active protein complexes Reviewed

    Crofts N, Abe N, Oitome NF, Matsushima R, Hayashi M, Tetlow IJ, Emes MJ, Nakamura Y, Fujita F

    Journal of Experimental Botany   66 ( 15 )   4469 - 4482   2015.8

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    Amylopectin is a highly branched, organized cluster of glucose polymers, and the major component of rice starch. Synthesis of amylopectin requires fine co-ordination between elongation of glucose polymers by soluble starch synthases (SSs), generation of branches by branching enzymes (BEs), and removal of misplaced branches by debranching enzymes (DBEs). Among the various isozymes having a role in amylopectin biosynthesis, limited numbers of SS and BE isozymes have been demonstrated to interact via protein-protein interactions in maize and wheat amyloplasts. This study investigated whether protein-protein interactions are also found in rice endosperm, as well as exploring differences between species. Gel permeation chromatography of developing rice endosperm extracts revealed that all 10 starch biosynthetic enzymes analysed were present at larger molecular weights than their respective monomeric sizes. SSIIa, SSIIIa, SSIVb, BEI, BEIIb, and PUL co-eluted at mass sizes &gt;700 kDa, and SSI, SSIIa, BEIIb, ISA1, PUL, and Pho1 co-eluted at 200-400 kDa. Zymogram analyses showed that SSI, SSIIIa, BEI, BEIIa, BEIIb, ISA1, PUL, and Pho1 eluted in high molecular weight fractions were active. Comprehensive co-immunoprecipitation analyses revealed associations of SSs-BEs, and, among BE isozymes, BEIIa-Pho1, and pullulanase-type DBE-BEI interactions. Blue-native-PAGE zymogram analyses confirmed the glucan-synthesizing activity of protein complexes. These results suggest that some rice starch biosynthetic isozymes are physically associated with each other and form active protein complexes. Detailed analyses of these complexes will shed light on the mechanisms controlling the unique branch and cluster structure of amylopectin, and the physicochemical properties of starch.

    DOI: 10.1093/jxb/erv212

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  • A Mutation in GIANT CHLOROPLAST Encoding a PARC6 Homolog Affects Spikelet Fertility in Rice Reviewed

    Kamau PK, Sano S, Takami T, Matsushima R, Maekawa M, Sakamoto W

    Plant and Cell Physiology   56 ( 5 )   977 - 991   2015.5

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    Chloroplasts are not generated de novo but proliferate from a pre-existing population of plastids present in meristematic cells. Chloroplast division is executed by the co-ordinated action of at least two molecular machineries: internal machinery located on the stromal side of the inner envelope membrane and external machinery located on the cytosolic side of the outer envelope membrane. To date, molecular studies of chloroplast division in higher plants have been limited to several species such as Arabidopsis. To elucidate chloroplast division in rice, we performed forward genetics and isolated a mutant displaying large chloroplasts among an ethyl methanesulfonate (EMS)-mutagenized Oryza sativa spp japonica Nipponbare population. Using a map-based approach, this mutation, termed giant chloroplast (gic), was allocated in a gene that encodes a protein that is homologous to Paralog of ARC6 (PARC6), which is known to play a role in chloroplast division. GIC is unique in that it has a long C-terminal extension that is not present in other PARC6 homologs. Characterization of gic phenotypes in a rice field showed that gic exhibited defective growth in seed setting, suggesting that the gic mutant negatively affects the reproductive stage. This report is the first describing a chloroplast division mutant in monocotyledons and its effect on plant development.

    DOI: 10.1093/pcp/pcv024

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  • Deficiencies in both starch synthase IIIa and branching enzyme IIb lead to a significant increase in amylose in SSIIa-inactive japonica rice seeds Reviewed

    Asai H, Abe N, Matsushima R, Crofts N, Oitome NF, Nakamura Y, Fujita N

    Journal of Experimental Botany   65 ( 18 )   5497 - 5507   2014.10

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    Starch synthase (SS) IIIa has the second highest activity of the total soluble SS activity in developing rice endosperm. Branching enzyme (BE) IIb is the major BE isozyme, and is strongly expressed in developing rice endosperm. A mutant (ss3a/be2b) was generated from wild-type japonica rice which lacks SSIIa activity. The seed weight of ss3a/be2b was 74-94% of that of the wild type, whereas the be2b seed weight was 59-73% of that of the wild type. There were significantly fewer amylopectin short chains [degree of polymerization (DP) &lt;= 13] in ss3a/be2b compared with the wild type. In contrast, the amount of long chains (DP &gt;= 25) connecting clusters of amylopectin in ss3a/be2b was higher than in the wild type and lower than in be2b. The apparent amylose content of ss3a/be2b was 45%, which was &gt;1.5 times greater than that of either ss3a or be2b. Both SSIIIa and BEIIb deficiencies led to higher activity of ADP-glucose pyrophosphorylase (AGPase) and granule-bound starch synthase I (GBSSI), which partly explains the high amylose content in the ss3a/be2b endosperm. The percentage apparent amylose content of ss3a and ss3a/be2b at 10 days after flowering (DAF) was higher than that of the wild type and be2b. At 20 DAF, amylopectin biosynthesis in be2b and ss3a/be2b was not observed, whereas amylose biosynthesis in these lines was accelerated at 30 DAF. These data suggest that the high amylose content in the ss3a/be2b mutant results from higher amylose biosynthesis at two stages, up to 20 DAF and from 30 DAF to maturity.

    DOI: 10.1093/jxb/eru310

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  • Amyloplast-Localized SUBSTANDARD STARCH GRAIN4 Protein Influences the Size of Starch Grains in Rice Endosperm Reviewed International journal

    Matsushima R*, Maekawa M, Kusano M, Kondo H, Fujita N, Kawagoe Y, Sakamoto W

    Plant Physiology   154 ( 2 )   2623 - 2636   2014.2

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC PLANT BIOLOGISTS  

    Abstract

    Starch is a biologically and commercially important polymer of glucose and is synthesized to form starch grains (SGs) inside amyloplasts. Cereal endosperm accumulates starch to levels that are more than 90% of the total weight, and most of the intracellular space is occupied by SGs. The size of SGs differs depending on the plant species and is one of the most important factors for industrial applications of starch. However, the molecular machinery that regulates the size of SGs is unknown. In this study, we report a novel rice (Oryza sativa) mutant called substandard starch grain4 (ssg4) that develops enlarged SGs in the endosperm. Enlargement of SGs in ssg4 was also observed in other starch-accumulating tissues such as pollen grains, root caps, and young pericarps. The SSG4 gene was identified by map-based cloning. SSG4 encodes a protein that contains 2,135 amino acid residues and an amino-terminal amyloplast-targeted sequence. SSG4 contains a domain of unknown function490 that is conserved from bacteria to higher plants. Domain of unknown function490-containing proteins with lengths greater than 2,000 amino acid residues are predominant in photosynthetic organisms such as cyanobacteria and higher plants but are minor in proteobacteria. The results of this study suggest that SSG4 is a novel protein that influences the size of SGs. SSG4 will be a useful molecular tool for future starch breeding and biotechnology.

    DOI: 10.1104/pp.113.229591

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  • Thin sections of Technovit 7100 resin of rice endosperm and staining Invited Reviewed

    Matsushima R*

    Bio-protocol   4   e1239   2014

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  • A phylogenetic re-evaluation of morphological variations of starch grains among Poaceae species Reviewed

    Matsushima R*, Yamashita* J, Kariyama S, Enomoto T, Sakamoto W

    Journal of Applied Glycoscience   60 ( 1 )   37 - 44   2013

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  • ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana Reviewed

    Nakano RT, Matsushima R, Nagano AJ, Fukao Y, Fujiwara M, Kondo M, Nishimura M, Hara-Nishimura I

    PLOS ONE   7 ( 11 )   e49103   2012.11

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    The endoplasmic reticulum (ER) has a unique, network-like morphology. The ER structures are composed of tubules, cisternae, and three-way junctions. This morphology is highly conserved among eukaryotes, but the molecular mechanism that maintains ER morphology has not yet been elucidated. In addition, certain Brassicaceae plants develop a unique ER-derived organelle called the ER body. This organelle accumulates large amounts of PYK10, a beta-glucosidase, but its physiological functions are still obscure. We aimed to identify a novel factor required for maintaining the morphology of the ER, including ER bodies, and employed a forward-genetic approach using transgenic Arabidopsis thaliana (GFP-h) with fluorescently-labeled ER. We isolated and investigated a mutant (designated endoplasmic reticulum morphology3, ermo3) with huge aggregates and abnormal punctate structures of ER. ERMO3 encodes a GDSL-lipase/esterase family protein, also known as MVP1. Here, we showed that, although ERMO3/MVP1/GOLD36 was expressed ubiquitously, the morphological defects of ermo3 were specifically seen in a certain type of cells where ER bodies developed. Coimmunoprecipitation analysis combined with mass spectrometry revealed that ERMO3/MVP1/GOLD36 interacts with the PYK10 complex, a huge protein complex that is thought to be important for ER body-related defense systems. We also found that the depletion of transcription factor NAI1, a master regulator for ER body formation, suppressed the formation of ER-aggregates in ermo3 cells, suggesting that NAI1 expression plays an important role in the abnormal aggregation of ER. Our results suggest that ERMO3/MVP1/GOLD36 is required for preventing ER and other organelles from abnormal aggregation and for maintaining proper ER morphology in a coordinated manner with NAI1.

    DOI: 10.1371/journal.pone.0049103

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  • Mutations defective in ribonucleotide reductase activity interfere with pollen plastid DNA degradation mediated by DPD1 exonuclease Reviewed

    Tang LY, Matsushima R, Sakamoto W

    Plant Journal   70 ( 4 )   637 - 649   2012.5

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

    Organellar DNAs in mitochondria and plastids are present in multiple copies and make up a substantial proportion of total cellular DNA despite their limited genetic capacity. We recently demonstrated that organellar DNA degradation occurs during pollen maturation, mediated by the Mg2+-dependent organelle exonuclease DPD1. To further understand organellar DNA degradation, we characterized a distinct mutant (dpd2). In contrast to the dpd1 mutant, which retains both plastid and mitochondrial DNAs, dpd2 showed specific accumulation of plastid DNAs. Multiple abnormalities in vegetative and reproductive tissues of dpd2 were also detected. DPD2 encodes the large subunit of ribonucleotide reductase, an enzyme that functions at the rate-limiting step of de novo nucleotide biosynthesis. We demonstrated that the defects in ribonucleotide reductase indirectly compromise the activity of DPD1 nuclease in plastids, thus supporting a different regulation of organellar DNA degradation in pollen. Several lines of evidence provided here reinforce our previous conclusion that the DPD1 exonuclease plays a central role in organellar DNA degradation, functioning in DNA salvage rather than maternal inheritance during pollen development.

    DOI: 10.1111/j.1365-313X.2012.04904.x

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  • 澱粉粒の簡便観察法の開発とその利用 Invited

    松島 良

    応用糖質科学   2   147 - 149   2012

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  • A Conserved, Mg2+-Dependent Exonuclease Degrades Organelle DNA during Arabidopsis Pollen Development Reviewed

    Ryo Matsushima, Lay Yin Tang, Lingang Zhang, Hiroshi Yamada, David Twell, Wataru Sakamoto

    Plant Cell   23 ( 4 )   1608 - 1624   2011.4

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    In plant cells, mitochondria and plastids contain their own genomes derived from the ancestral bacteria endosymbiont. Despite their limited genetic capacity, these multicopy organelle genomes account for a substantial fraction of total cellular DNA, raising the question of whether organelle DNA quantity is controlled spatially or temporally. In this study, we genetically dissected the organelle DNA decrease in pollen, a phenomenon that appears to be common in most angiosperm species. By staining mature pollen grains with fluorescent DNA dye, we screened Arabidopsis thaliana for mutants in which extrachromosomal DNAs had accumulated. Such a recessive mutant, termed defective in pollen organelle DNA degradation1 (dpd1), showing elevated levels of DNAs in both plastids and mitochondria, was isolated and characterized. DPD1 encodes a protein belonging to the exonuclease family, whose homologs appear to be found in angiosperms. Indeed, DPD1 has Mg2+-dependent exonuclease activity when expressed as a fusion protein and when assayed in vitro and is highly active in developing pollen. Consistent with the dpd phenotype, DPD1 is dual-targeted to plastids and mitochondria. Therefore, we provide evidence of active organelle DNA degradation in the angiosperm male gametophyte, primarily independent of maternal inheritance; the biological function of organellar DNA degradation in pollen is currently unclear.

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  • Interaction between Phaseolus plants and two strains of Kanzawa spider mites Reviewed

    Ozawa R, Matsushima R, Maffei M, Takabayashi J

    Journal of Plant Interactions   6 ( 2-3 )   125 - 128   2011

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    Kanzawa spider mites, Tetranychus kanzawai, are polyphagous herbivores that feed on various plant families including legumes. Lima bean leaves infested by T. kanzawai emit a specific blend of volatiles. We found that two strains of spider mites were able to induce different blends of volatile to lima bean plants infested by either strain. Here we describe the genetic properties of the two strains and the responses of lima bean plants to the mite damage in terms of expression of defensive genes, emission of herbivore-induced plant volatiles, and phenotypic response of lima bean and other legume leaves (leaf color).

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  • A Rapid, Direct Observation Method to Isolate Mutants with Defects in Starch Grain Morphology in Rice Reviewed

    Matsushima R*, Maekawa M, Fujita N, Sakamoto W

    Plant and Cell Physiology   51 ( 5 )   728 - 741   2010.5

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    Starch forms transparent grains, referred to as starch grains (SGs), in amyloplasts. Despite the simple glucose polymer composition of starch, SGs exhibit different morphologies depending on plant species, especially in the endosperm of the Poaceae family. This study reports a novel method for preparing thin sections of endosperm without chemical fixation or resin embedding that allowed us to visualize subcellular SGs clearly. Using this method, we observed the SG morphologies of 5,000 mutagenized rice seeds and were able to isolate mutants in which SGs were morphologically altered. In five mutants, named ssg (substandard starch grain), increased numbers of small SGs (ssg1ssg3), enlarged SGs (ssg4) and abnormal interior structures of SGs (ssg5) were observed. Amylopectin chain length distribution analysis and identification of the mutated gene suggested a possible allelic relationship between ssg1, ssg2, ssg3 and the previously isolated amylose-extender (ae) mutants, while ssg4 and ssg5 seemed to be novel mutants. Compared with conventional observation methods, the methods developed here are more effective for obtaining fine images of subcellular SGs and are suitable for the observation of a large number of samples.

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

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

    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.

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  • Visualization of Plastids in Pollen Grains: Involvement of FtsZ1in Pollen Plastid Division Reviewed

    Tang LY, Nagata N, Matsushima R, Chen Y, Yoshioka Y, Sakamoto W

    Plant and Cell Physiology   50 ( 4 )   904 - 908   2009.4

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    Visualizing organelles in living cells is a powerful method to analyze their intrinsic mechanisms. Easy observation of chlorophyll facilitates the study of the underlying mechanisms in chloroplasts, but not in other plastid types. Here, we constructed a transgenic plant enabling visualization of plastids in pollen grains. Combination of a plastid-targeted fluorescent protein with a pollen-specific promoter allowed us to observe the precise number, size and morphology of plastids in pollen grains of the wild type and the ftsZ1 mutant, whose responsible gene plays a central role in chloroplast division. The transgenic material presented in this work is useful for studying the division mechanism of pollen plastids.

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  • Mitochondrial dynamics in plant male gametophyte visualized by fluorescent live imaging Reviewed

    Matsushima R, Hamamura Y, Higashiyama T, Arimura S-i, Sodmergen, Tsutsumi N, Sakamoto W

    Plant and Cell Physiology   49 ( 7 )   1074 - 1083   2008.7

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    Visualization of organelles in living cells is a powerful method for studying their dynamic behavior. Here we attempted to visualize mitochondria in angiosperm male gametophyte (pollen grain from Arabidopsis thaliana) that are composed of one vegetative cell (VC) and two sperm cells (SCs). Combination of mitochondria-targeted fluorescent proteins with VC- or SC-specific expression allowed us to observe the precise number and dynamic behavior of mitochondria in the respective cell types. Furthermore, live imaging of SC mitochondria during double fertilization confirmed previous observations, demonstrated by electron microscopy in other species, that sperm mitochondria enter into the egg and central cells. We also attempted to visualize mutant mitochondria that were elongated due to a defect in mitochondrial division. This mutant phenotype was indeed detectable in VC mitochondria of a heterozygous F(1) plant, suggesting active mitochondrial division in male gametophyte. Finally, we performed mutant screening and isolated a putative mitochondrial protein transport mutant whose phenotype was detectable only in haploid cells. The transgenic materials presented in this work are useful not only for live imaging but also for studying mitochondrial functions by mutant analysis.

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  • The model plant Medicago truncatula exhibits biparental plastid inheritance Reviewed

    Matsushima R, Hu Y, Toyoda K, Sodmergen, Sakamoto W

    Plant and Cell Physiology   49 ( 1 )   81 - 91   2008.1

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    The plastid, which originated from the endosymbiosis of a cyanobacterium, contains its own plastid DNA (ptDNA) that exhibits a unique mode of inheritance. Approximately 80 of angiosperms show maternal inheritance, whereas the remainder exhibit biparental inheritance of ptDNA. Here we studied ptDNA inheritance in the model legume, Medicago truncatula. Cytological analysis of mature pollen with DNA-specific fluorescent dyes suggested that M. truncatula is one of the few model plants potentially showing biparental inheritance of ptDNA. We further examined pollen by electron microscopy and revealed that the generative cell (a mother of sperm cells) indeed has many DNA-containing plastids. To confirm biparental inheritance genetically, we crossed two ecotypes (Jemalong A17 and A20), and the transmission mode of ptDNA was investigated by a PCR-assisted polymorphism. Consistent with the cytological observations, the majority of F-1 plants possessed ptDNAs from both parents. Interestingly, cotyledons of F-1 plants tended to retain a biparental ptDNA population, while later emergent leaves tended to be uniparental with either one of the parental plastid genotypes. Biparental transmission was obvious in the F-2 population, in which all plants showed homoplasmy with either a paternal or a maternal plastid genotype. Collectively, these data demonstrated that M. truncatula is biparental for ptDNA transmission and thus can be an excellent model to study plastid genetics in angiosperms.

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  • White leaf sectors in yellow variegated2 are formed by viable cells with undifferentiated plastids Reviewed

    Kato Y, Miura E, Matsushima R, Sakamoto W

    Plant Physiology   144 ( 2 )   952 - 960   2007.6

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    The yellow variegated2 (var2) is one of the best- characterized Arabidopsis (Arabidopsis thaliana) mutants showing leaf variegation. Leaf variegation of var2 results from the loss of an ATP-dependent metalloprotease, FtsH2, which is a major component of the FtsH heterocomplex in thylakoid membranes. While the functional role of FtsH2 in protein quality control has been extensively studied, the physiological state of plastids in white tissues of the var2 is not well characterized. Here we show that the white tissue in var2 is neither the result of photobleaching nor enhanced senescence. Visualization of plastids by plastid-targeted green fluorescent protein revealed that plastids in the white sector are distinct and have undifferentiated characteristics. The plastids are also distinct in that they contain large nucleoids, a complex structure of plastid DNA and proteins, that are typically found in undifferentiated plastids. Comparative analyses of protein profiles from green and white tissues suggested that the difference was observed in the proteins related to photosynthesis but not due to proteins of other organelles. Thus, cells in the white tissue are viable and their defect is limited to plastid function. The plastid accumulates normal levels of chloroplast transcripts, whereas a substantial repression of nuclear-encoded photosynthetic genes was evident in the white sector. Based upon these results, we inferred that the white sectors in var2 are made by viable cells that have plastids arrested in thylakoid formation. A proposed model to form the variegated sector in var2 is provided.

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  • The balance between protein synthesis and degradation in chloroplasts determines leaf variegation in Arabidopsis yellow variegated mutants Reviewed

    Miura E, Kato Y, Matsushima R, Albrecht V, Laalami S, Sakamoto W

    Plant Cell   19 ( 4 )   1313 - 1328   2007.4

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    An Arabidopsis thaliana leaf-variegated mutant yellow variegated2 (var2) results from loss of FtsH2, a major component of the chloroplast FtsH complex. FtsH is an ATP-dependent metalloprotease in thylakoid membranes and degrades several chloroplastic proteins. To understand the role of proteolysis by FtsH and mechanisms leading to leaf variegation, we characterized the second-site recessive mutation fu-gaeri1 (fug1) that suppressed leaf variegation of var2. Map-based cloning and subsequent characterization of the FUG1 locus demonstrated that it encodes a protein homologous to prokaryotic translation initiation factor 2 (cpIF2) located in chloroplasts. We show evidence that cpIF2 indeed functions in chloroplast protein synthesis in vivo. Suppression of leaf variegation by fug1 is observed not only in var2 but also in var1 (lacking FtsH5) and var1 var2. Thus, suppression of leaf variegation caused by loss of FtsHs is most likely attributed to reduced protein synthesis in chloroplasts. This hypothesis was further supported by the observation that another viable mutation in chloroplast translation elongation factor G also suppresses leaf variegation in var2. We propose that the balance between protein synthesis and degradation is one of the determining factors leading to the variegated phenotype in Arabidopsis leaves.

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  • Intraspecies variation in the Kanzawa spider mite differentially affects induced defensive response in lima bean plants Reviewed

    Matsushima R, Ozawa R, Uefune M, Gotoh T, Takabayashi J

    Journal of Chemical Ecology   32 ( 11 )   2501 - 2512   2006.11

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    The Kanzawa spider mite, Tetranychus kanzawai, is a polyphagous herbivore that feeds on various plant families, including the Leguminacae. Scars made by the mite on lima bean leaves (Phaseolus lunatus) were classified into two types: white and red. We obtained two strains of mites - "White" and "Red" - by selecting individual mites based on the color of the scars. Damage made by the Red strain induced the expression of genes for both basic chitinase, which was downstream of the jasmonic acid (JA) signaling pathway, and acidic chitinase, which was downstream of the salicylic acid (SA) signaling pathway. White strain mites also induced the expression of the basic chitinase gene in infested leaves but they only slightly induced the acidic chitinase gene. The Red genotype was dominant over the White for the induction of the acidic chitinase gene. The amount of endogenous salicylates in leaves increased significantly when infested by Red strain mites but did not increase when infested by White strain mites. JA and SA are known to be involved in the production of lima bean leaf volatiles induced by T. urticae. The blend of volatiles emitted from leaves infested by the Red strain were qualitatively different from those infested by the White strain, suggesting that the SA and JA signaling pathways are differently involved in the production of lima bean leaf volatiles induced by T. kanzawai of different strains.

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  • Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana Reviewed

    Nagano AJ, Matsushima R, Hara-Nishimura I

    Plant and Cell Physiology   46 ( 7 )   1140 - 1148   2005.7

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    The ER body is an endoplasmic reticulum (ER)derived organelle. Because ER bodies are induced by wounding and methyl jasmonate (MeJA) treatment in rosette leaves, they might be responsible for defense systems. Recently, we isolated nail mutants that have no ER body and showed that the levels of PYK10 and PBP1 (PYK10-binding protein 1: At3g16420) were decreased in nail mutants. PYK10 is a beta-glucosidase that is localized in ER bodies. PBP1 consists of two repeated regions, each of which is highly homologous to the a-chain of jacalin, a carbohydrate-binding protein (lectin) of Artocarpus integriforia. We show in this study that PYK10 has two forms, an active form and an inactive form. The amount of active form increased during incubation of root homogenate. On the other hand, PYK10 separated into soluble and insoluble forms. Active PYK10 molecules mainly occurred as the insoluble form and inactive PYK10 molecules remain soluble. This suggests that the activation of PYK10 needs polymerization. In homogenates of both a pbp1 mutant and the wild type, PYK10 becomes insoluble, while PYK10 activity in pbp1 is only half of that in the wild type. PBP1 has an ability to interact with PYK10. Nonetheless, PBP1 does not bind active PYK10. These results suggest that PBP1 has some effect on the activation of PYK10. In addition, PBP1 was found to have a different subcellular distribution from PYK10. PBP1 may act like a molecular chaperone that facilitates the correct polymerization of PYK10, when tissues are damaged and subcellular structures are destroyed by pests.

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  • Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells? Reviewed

    Hara-Nishimura I, Matsushima R, Shimada T, Nishimura M

    Plant Physiology   136 ( 3 )   3435 - 3439   2004.11

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  • NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body Reviewed

    Matsushima R, Fukao Y, Nishimura M, Hara-Nishimura I

    Plant Cell   16 ( 6 )   1536 - 1549   2004.6

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    Plant cells develop various types of endoplasmic reticulum (ER)-derived structures with specific functions. ER body, an ER-derived compartment in Arabidopsis thaliana, is a spindle-shaped structure. The NAI1 gene regulates the development of ER bodies because mutation of NAI1 abolishes the formation of ER bodies. To better understand the role of NAI1, we cloned the NAI1 gene using a positional cloning strategy. The nai1-1 mutant had a single nucleotide change at an intron acceptor site of At2g22770 (NAI1 gene). Because of this mutation, aberrant splicing of NAI1 mRNA occurs in the nai1-1 mutant. NAI1 encodes a transcription factor that has a basic-helix-loop-helix (bHLH) domain. Transient expression of NAI1 induced ER bodies in the nai1-1 mutant. Two-dimensional electrophoresis and RT-PCR analyses showed that a putative lectin was depressed at both the mRNA and protein levels in nail mutants, as was a beta-glucosidase (PYK10). Our results provide direct evidence that a bHLH protein plays a role in the formation of ER bodies.

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  • An ER-Localized form of PV72, a seed-specific vacuolar sorting receptor, interferes the transport of an NPIR-containing proteinase in Arabidopsis leaves Reviewed

    Watanabe E, Shimada T, Tamura K, Matsushima R, Koumoto Y, Nishimura M, Hara-Nishimura I

    Plant and Cell Physiology   45 ( 1 )   9 - 17   2004.1

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    Putative vacuolar sorting receptors that bind to the vacuolar targeting signals have been found in various plants; pumpkin PV72, pea BP-80 and Arabidopsis AtELP. PV72 is a seed-specific receptor that is predicted to sort seed storage proteins to protein storage vacuoles. Analysis by surface plasmon resonance showed that the lumenal domain of PV72 bound to an NPIR (a typical vacuolar targeting signal)-containing peptide of the precursor of a cysteine proteinase, AtALEU, in the presence of Ca2+ (K-D = 0.1 muM). To elucidate the receptor-dependent transport of vacuolar proteins in plant cells, we produced transgenic Arabidopsis plants that expressed a fusion protein (PV72-HDEL) composed of the lumenal domain of PV72 and an endoplasmic reticulum (ER)-retention signal, HDEL. The expression of PV72-HDEL induced the accumulation of the AtALEU precursor. The accumulation level of the AtALEU precursor was dependent on that of PV72-HDEL. In contrast, it did not induce the accumulation of a precursor of another cysteine proteinase, RD21, which contains no NPIR. Detailed subcellular localization revealed that both the AtALEU precursor and PV72-HDEL accumulated in the ER fraction. We found that most of the AtALEU precursor molecules formed a complex with PV72-HDEL. The AtALEU precursor might be trapped by PV72-HDEL in the ER and not transported to the vacuoles. This in-planta analysis supports the hypothesis that an Arabidopsis homolog of PV72 functions as a sorting receptor for the NPIR-containing proteinase. The overall results suggest that vacuolar sorting receptors for the protein storage vacuoles and the lytic vacuoles share the similar recognition mechanism for a vacuolar targeting signal.

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  • A wound-inducible organelle derived from endoplasmic reticulum: a plant strategy against environmental stresses? Reviewed

    Hara-Nishimura I, Matsushima R

    Current Opinion in Plant Biology   6 ( 6 )   583 - 588   2003.12

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    Endoplasmic reticulum (ER) is the most multitalented and adaptable compartment in plant cells. Recently, a wound-inducible organelle, which is derived from ER and designated the ER body, was found in Arabidopsis. Wounding and methyl jasmonate induce many ER bodies in rosette leaves, which have no ER bodies under normal conditions. In contrast, tender seedlings have a wide distribution of the ER bodies especially in all the epidermal cells, which are easily stressed by the external environment. The ER bodies play a role in a novel and unique type of endomembrane system that is involved in the response of plant cells to environmental stress and wounding.

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

    Matsushima R, Hayashi Y, Yamada K, Shimada T, Nishimura M, 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.

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  • A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis Reviewed

    Matsushima R, Kondo M, Nishimura M, Hara-Nishimura I

    Plant Journal   33 ( 3 )   493 - 502   2003.2

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    The ER body is a novel compartment that is derived from endoplasmic reticulum (ER) in Arabidopsis . In contrast to whole seedlings which have a wide distribution of the ER bodies, rosette leaves have no ER bodies. Recently, we reported that wound stress induces the formation of many ER bodies in rosette leaves, suggesting that the ER body plays a role in the defense system of plants. ER bodies were visualized in transgenic plants (GFP-h) expressing green fluorescent protein (GFP) with an ER-retention signal, HDEL. These were concentrated in a 1000-g pellet (P1) of GFP-h plants. We isolated an Arabidopsis mutant, nai1, in which fluorescent ER bodies were hardly detected in whole plants. We found that a 65-kDa protein was specifically accumulated in the P1 fraction of GFP-h plants, but not in the P1 fraction of nai1 plants. N-terminal peptide sequencing revealed that the 65-kDa protein was a beta-glucosidase, PYK10, with an ER-retention signal, KDEL. Immunocytochemistry showed that PYK10 was localized in the ER bodies. Compared with the accumulation of GFP-HDEL, which was associated with both cisternal ER and ER bodies, the accumulation of PYK10 was much more specific to ER bodies. PYK10 was one of the major proteins in cotyledons, hypocotyls and roots of Arabidopsis seedlings, while PYK10 was not detected in rosette leaves that have no ER bodies. These findings indicated that PYK10 is the main component of ER bodies. It is possible that PYK10 produces defense compounds when plants are damaged by insects or wounding.

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

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

    Plant Physiology   130 ( 4 )   1807 - 1814   2002.12

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    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.

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  • A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves.

    Yamada K, Matsushima R, Nishimura M, Hara-Nishimura I

    Plant Physiology   127   1626 - 1634   2001.12

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    Arabidopsis RD21 is a cysteine protease of the papain family. Unlike other members of the papain family, RD21 has a C-terminal extension sequence composed of two domains, a 2-kD proline-rich domain and a 10-kD domain homologous to animal epithelin/granulin family proteins. The RD21 protein was accumulated as 38- and 33-kD proteins in Arabidopsis leaves. An immunoblot showed that the 38-kD protein had the granulin domain, whereas the 33-kD protein did not. A pulse-chase experiment with Bright-Yellow 2 transformant cells expressing RD21 showed that RD21 was synthesized as a 57-kD precursor and was then slowly processed to make the 33-kD mature protein via the 38-kD intermediate. After a 12-h chase, the 38-kD intermediate was still detected in the cells. These results indicate that the N-terminal propeptide was first removed from the 57-kD precursor, and the C-terminal granulin domain was then slowly removed to yield the 33-kD mature protein. Subcellular fractionation of the Bright-Yellow 2 transformant showed that the intermediate and mature forms of RD21 were localized in the vacuoles. Under the acidic conditions of the vacuolar interior, the intermediate was found to be easily aggregated. The intermediate and the mature protein were accumulated in association with leaf senescence. Taken together, these results indicate that the intermediate of RD21 was accumulated in the vacuoles as an aggregate, and then slowly matured to make a soluble protease by removing the granulin domain during leaf senescence.

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

    Hayashi Y, Yamada K, Shimada T, Matsushima R, Nishizawa NK, Nishimura M, 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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  • Analysis of morphological changes in carrot somatic embryogenesis by serial observation Reviewed

    Ibaraki Y, Matsushima R, Kurata K

    Plant Cell, Tissue and Organ Culture   61 ( 1 )   9 - 14   2000

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:KLUWER ACADEMIC PUBL  

    Carrot somatic embryogenesis was serially observed using a cell cluster immobilizing system with Phytagel. Embryogenic cell clusters ranging in size from 32 to 63 mu m were collected by filtration and used for somatic embryo induction. Of the 432 cell clusters, 253 grew, i.e., the size of these cell clusters increased, and 192 developed into globular embryos. Through serial observation, the number of somatic embryos produced from each cell cluster was identified. Cell clusters which developed into two or more embryos grew and developed slowly as compared with cell clusters which developed into single embryos. Serial observation also revealed that some cell clusters consisted of several parts, each of which independently grew as separate units. In cases where two growing parts fused into one embryo, morphological abnormalities such as curvature or lumps in their bodies were occasionally observed.

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Books

  • Morphological variations of starch grains. in Starch: Metabolism and Structure.

    Matsushima R( Role: Joint author ,  425-441)

    Y. Nakamura, ed (Springer Japan)  2015 

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  • 植物の小胞体由来の構造体

    松島 良, 嶋田知生, 西村いくこ( Role: Joint author ,  293-298)

    プラントミメティックス〜植物に学ぶ〜 エヌ・ティー・エス株式会社  2006 

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  • ジャスモン酸メチルによって誘導される小胞体由来の新奇構造体

    松島良, 西村いくこ( Role: Joint author ,  209-212)

    細胞工学別冊 植物細胞工学シリーズ「新版 植物ホルモンのシグナル伝達」秀潤社  2004 

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Presentations

  • Genetic interactions of starch-related mutations differ between endosperm and pollen

    2024.3.17 

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    Event date: 2024.3.16 - 2024.3.17

    Language:Japanese   Presentation type:Oral presentation (general)  

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  • 穀類胚乳の澱粉合成に関する 遺伝学的研究

    松島 良

    第39回資源植物科学シンポジウム及び 第15回植物ストレス科学研究シンポジウム 植物科学の 基礎から応用まで  2024.2.26 

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    Event date: 2024.2.26 - 2024.2.27

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  • Analysis of multiple mutants of starch-related genes in barley

    2023.12.23 

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    Event date: 2023.12.23 - 2023.12.24

    Language:Japanese   Presentation type:Poster presentation  

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  • FLOURY ENDOSPERM 6 mutations enhance the sugary phenotype caused by the loss of ISOAMYLASE1 in barley

    Matsushima R, Hisano H, Galis I, Fujita N, Sato K

    The 3rd Barley Mutant Conference (3BMC)  2023.10.8 

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    Event date: 2023.10.9 - 2023.10.10

    Language:English   Presentation type:Poster presentation  

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  • Genetic interaction of starch-related mutations using barley multiple mutants

    2023.3.17 

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    Event date: 2023.3.17 - 2023.3.18

    Language:Japanese   Presentation type:Oral presentation (general)  

    File: 143program.pdf

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  • オオムギ多重変異体を用いた澱粉関連遺伝子の遺伝的相互作用解析

    松島 良, 久野 裕, Ivan Galis, 三浦聡子, クロフツ尚子, 追留那緒子, 藤田直子, 佐藤和広

    第17回ムギ類研究会 

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    Event date: 2022.12.16 - 2022.12.17

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  • オオムギうどんこ病菌侵入細胞におけるプラスチド崩壊メカニズムの解析

    在間 玄香, 井上 博, 久野 裕, 松島 良, 小林 括平, 山岡 直人, 中神 弘史, 八丈野 孝

    日本植物学会第 86 回大会 

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    Event date: 2022.9.17 - 2022.9.19

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  • Development of barley mutant with reduced starch and high sugar accumulation

    2022.3.20 

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    Event date: 2022.3.20 - 2022.3.21

    Language:Japanese  

  • Development of barley mutant with reduced starch and high sugar accumulation

    2022.3.20 

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    Event date: 2022.3.20 - 2022.3.21

    Language:Japanese   Presentation type:Poster presentation  

    File: 141program.pdf

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  • 澱粉粒の形状多様性と オオムギの種子澱粉改変に向けての取り組み

    松島 良

    第2回植物研究拠点アライアンス公開シンポジウム  2022.1.27 

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    Event date: 2022.1.27

    Language:Japanese  

  • 澱粉粒の形状多様性と オオムギの種子澱粉改変に向けての取り組み

    松島 良

    第2回植物研究拠点アライアンス公開シンポジウム  2022.1.27 

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    Event date: 2022.1.27

    Language:Japanese   Presentation type:Symposium, workshop panel (nominated)  

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  • Isolation of barley mutant with reduced starch and high accumulation of sugars

    2021.12.25 

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    Event date: 2021.12.25

    Language:Japanese  

  • Isolation of barley mutant with reduced starch and high accumulation of sugars

    2021.12.25 

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    Event date: 2021.12.25

    Language:Japanese   Presentation type:Poster presentation  

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  • Cytological studies of starch grain morphologies of cereals - Towards the understanding of the morphological diversity of starch grains. (Invited lecture) Invited

    Ryo Matsushima

    2021 Starch Round Table  2021.10.4 

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    Event date: 2021.10.4 - 2021.10.8

    Language:English  

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  • 澱粉蓄積量可変のオオムギの開発と機能性多糖の蓄積への応用

    松島 良

    岡山大学 新技術説明会  2021.9.30 

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    Event date: 2021.9.30

    Language:Japanese   Presentation type:Oral presentation (general)  

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  • 澱粉粒の形状に異常を示すオオムギ突然変異体の表現型解析

    松島 良, 久野 裕, 追留那緒子, 藤田直子, 佐藤和広

    第15回ムギ類研究会  2020.12.26 

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    Event date: 2020.12.26

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  • 澱粉粒の形状に異常を示すオオムギ突然変異体の澱粉特性評価

    松島 良, 久野 裕, 追留那緒子, 藤田直子, 佐藤和広

    第12回中国地域育種談話会  2020.12.12 

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    Event date: 2020.12.12

    Language:Japanese  

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  • 澱粉粒の形状に異常を示すオオムギ突然変異体の遺伝学的解析

    松島 良, 久野 裕, 三浦聡子, 保坂優子, 追留那緒子, 高橋里香, 藤田直子, 佐藤和広

    日本育種学会 第138回講演会  2020.10.11 

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    Event date: 2020.10.10 - 2020.10.11

    Language:Japanese  

    File: 138program.pdf

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  • スターチシンターゼ(SS)IIaと枝作り酵素(BE)IIbの二重変異体米が登熟胚乳で形成する澱粉生合成関連酵素の超高分子量タンパク質複合体の解析

    井田圭美, クロフツ尚子, 三浦聡子, 保坂優子, 松島良, 藤田直子

    日本育種学会第138回講演会 

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    Event date: 2020.10.10 - 2020.10.11

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  • 病原菌侵入による宿主表皮プラスチド内デンプンの動態変化の解析

    井上博, 久野裕, 松島良, 小林括平, 山岡直人, 西内 巧, 中神弘史, 八丈野孝

    日本植物学会第84回大会  2020.9 

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    Event date: 2020.9.19 - 2020.9.21

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  • スターチシンターゼ(SS)IIaと枝作り酵素(BE)IIbの二重変異体米の澱粉構造とその性質

    井田圭美, クロフツ尚子, 三浦聡子, 保坂優子, 松島良, 藤田直子

    日本応用糖質科学会令和2年度大会(第69回) 

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    Event date: 2020.9.9 - 2020.9.10

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  • イネデンプン構造変異系統の胚乳特性解析および原因遺伝子探索

    永松志朗, 和田卓也, 松島良, 藤田直子, 三浦聡子, クロフツ尚子, 保坂優子, 熊丸敏博

    日本育種学会第137回講演会 

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    Event date: 2020.3.28 - 2020.3.29

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  • 難消化性澱粉を保有するイネ澱粉構造変異系統の胚乳特性解析

    和田卓也, 松島良, 藤田直子, 三浦聡子, クロフツ尚子, 保坂優子, 永松志朗, 熊丸敏博

    第68回日本応用糖質科学会 

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    Event date: 2019.9.11 - 2019.9.13

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  • 難消化性澱粉を多く含み,澱粉構造が異なる5つの枝作り酵素(BE)IIb変異体米の解析

    三浦 聡子, 菊池 佳奈, クロフツ 尚子, 保坂 優子, 阿部 美里, 松島 良, 藤田 直子

    第68回日本応用糖質科学会 

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    Event date: 2019.9.11 - 2019.9.13

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  • 澱粉粒の形状が変化したオオムギ突然変異体の単離と解析

    松島 良, 久野 裕, 藤田直子, 佐藤和広

    日本育種学会 第136回講演会  2019.9.7 

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    Event date: 2019.9.6 - 2019.9.7

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  • 難消化性澱粉(RS)を多く含む「ちくし粉85号」の胚乳澱粉及び 澱粉生合成関連酵素の解析

    三浦 聡子, クロフツ 尚子, 保坂 優子, 松島 良, 和田卓也, 藤田 直子

    日本応用糖質科学会東北支部会 

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    Event date: 2019.7.20

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  • Cytological and genetic studies of starch granule morphology using barley Invited

    Matsushima, R

    Biochemistry and Metabolism Special Seminar at John Inness Centre  2022.11.22 

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  • オオムギを用いた澱粉粒形状決定機構についての 細胞生物学的研究

    松島 良, 久野 裕, 佐藤和広

    第1回オオムギ資源開発研究セミナー  2018.12.7 

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  • Comparative imaging analysis of amyloplasts in rice and barley endosperm

    2018.9.23 

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  • 植物細胞の中で澱粉粒の形はいかに決定されるのか? Invited

    松島 良

    第65回 日本食品科学工学会  2018.8.24 

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Social Activities

  • 大原サマーサイエンスインターンシップ

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    2023.8.29 - 2023.9.1

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  • 令和4年度倉敷市大学連携講座

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    顕微鏡でのぞくデンプンの世界  2022.10.1

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    2022.9.5 - 2022.9.8

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    2022.8.1

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