ID | 63421 |
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Nagao, Ryo
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Kato, Koji
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Kumazawa, Minoru
Graduate School of Biostudies, Kyoto University
Ifuku, Kentaro
Graduate School of Agriculture, Kyoto University
Yokono, Makio
Institute of Low Temperature Science, Hokkaido University
Suzuki, Takehiro
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Dohmae, Naoshi
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Akita, Fusamichi
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Akimoto, Seiji
Graduate School of Science, Kobe University
Miyazaki, Naoyuki
Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba
Shen, Jian-Ren
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Abstract | Fucoxanthin chlorophyll (Chl) a/c-binding proteins (FCPs) function as light harvesters in diatoms. The structure of a diatom photosystem II-FCPII (PSII-FCPII) supercomplex have been solved by cryo-electron microscopy (cryo-EM) previously; however, the FCPII subunits that constitute the FCPII tetramers and monomers are not identified individually due to their low resolutions. Here, we report a 2.5 angstrom resolution structure of the PSII-FCPII supercomplex using cryo-EM. Two types of tetrameric FCPs, S-tetramer, and M-tetramer, are identified as different types of hetero-tetrameric complexes. In addition, three FCP monomers, m1, m2, and m3, are assigned to different gene products of FCP. The present structure also identifies the positions of most Chls c and diadinoxanthins, which form a complicated pigment network. Excitation-energy transfer from FCPII to PSII is revealed by time-resolved fluorescence spectroscopy. These structural and spectroscopic findings provide insights into an assembly model of FCPII and its excitation-energy transfer and quenching processes. Fucoxanthin chlorophyll a/c-binding proteins (FCPs) harvest light energy in diatoms. The authors analyzed a structure of PSII-FCPII supercomplex at high resolution by cryo-EM, which identified each FCP subunit and pigment network in the supercomplex.
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Published Date | 2022-04-01
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Publication Title |
Nature Communications
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Volume | volume13
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Issue | issue1
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Publisher | Nature Portfolio
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Start Page | 1764
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ISSN | 2041-1723
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | © The Author(s) 2022
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File Version | publisher
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Related Url | isVersionOf https://doi.org/10.1038/s41467-022-29294-5
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License | http://creativecommons.org/licenses/by/4.0/
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Funder Name |
Japan Society for the Promotion of Science
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助成番号 | JP20K06528
JP21K19085
JP20H02914
JP20H031160
JP20H03194
JP16H06553
JP17H06433
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