ID | 65542 |
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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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Hamaguchi, Tasuku
Biostructural Mechanism Laboratory, RIKEN SPring-8 Center
Ueno, Yoshifumi
Graduate School of Science, Kobe University
Tsuboshita, Naoki
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Shimizu, Shota
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
Furutani, Miyu
Graduate School of Science, Kobe University
Ehira, Shigeki
Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University
Nakajima, Yoshiki
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
ORCID
Kawakami, Keisuke
Biostructural Mechanism Laboratory, RIKEN SPring-8 Center
Suzuki, Takehiro
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Dohmae, Naoshi
Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Akimoto, Seiji
Graduate School of Science, Kobe University
Yonekura, Koji
Biostructural Mechanism Laboratory, RIKEN SPring-8 Center
Shen, Jian-Ren
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Abstract | Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from IsiAs to PSI appeared with a time constant of 55 ps. These findings provide insights into both the molecular assembly of the Anabaena IsiA family and the functional roles of IsiAs.
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Note | The version of record of this article, first published in Nature Communications, is available online at Publisher’s website: http://dx.doi.org/10.1038/s41467-023-36504-1
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Published Date | 2023-02-17
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Publication Title |
Nature Communications
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Volume | volume14
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Issue | issue1
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Publisher | Nature Portfolio
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Start Page | 920
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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) 2023
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File Version | publisher
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Related Url | isVersionOf https://doi.org/10.1038/s41467-023-36504-1
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License | http://creativecommons.org/licenses/by/4.0/
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Citation | Nagao, R., Kato, K., Hamaguchi, T. et al. Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120. Nat Commun 14, 920 (2023). https://doi.org/10.1038/s41467-023-36504-1
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Funder Name |
Japan Society for the Promotion of Science
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助成番号 | JP20H02914
JP21K19085
JP20K06528
JP17H06434
JP22H04916
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