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ID 48700
フルテキストURL
著者
Nagao, Ryo Department of Life Sciences (Biology), Graduate School of Art and Sciences, University of Tokyo
Moriguchi, Akira Department of Biology, Faculty of Science, Tokyo University of Science
Tomo, Tatsuya Department of Biology, Faculty of Science, Tokyo University of Science
Niikura, Ayako Division of Biosciences, Graduate School of Natural Science and Technology, Okayama University
Nakajima, Saori Department of Biology, Faculty of Science, Tokyo University of Science
Suzuki, Takehiro Biomolecular Characterization Team, Discovery Research Institute, RIKEN
Okumura, Akinori Department of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University
Iwai, Masako Department of Life Sciences (Biology), Graduate School of Art and Sciences, University of Tokyo
Shen, Jian-Ren Division of Biosciences, Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Ikeuchi, Masahiko Department of Life Sciences (Biology), Graduate School of Art and Sciences, University of Tokyo
Enami, Isao Department of Biology, Faculty of Science, Tokyo University of Science
抄録
Oxygen-evolving photosystem II (PSII) isolated from a marine centric diatom, Chaetoceros gracilis, contains a novel extrinsic protein (Psb31) in addition to four red algal type extrinsic proteins of PsbO, PsbQ′, PsbV, and PsbU. In this study, the five extrinsic proteins were purified from alkaline Tris extracts of the diatom PSII by anion and cation exchange chromatographic columns at different pH values. Reconstitution experiments in various combinations with the purified extrinsic proteins showed that PsbO, PsbQ′, and Psb31 rebound directly to PSII in the absence of other extrinsic proteins, indicating that these extrinsic proteins have their own binding sites in PSII intrinsic proteins. On the other hand, PsbV and PsbU scarcely rebound to PSII alone, and their effective bindings required the presence of all of the other extrinsic proteins. Interestingly, PSII reconstituted with Psb31 alone considerably restored the oxygen evolving activity in the absence of PsbO, indicating that Psb31 serves as a substitute in part for PsbO in supporting oxygen evolution. A significant difference found between PSIIs reconstituted with Psb31 and with PsbO is that the oxygen evolving activity of the former is scarcely stimulated by Cl− and Ca2+ ions but that of the latter is largely stimulated by these ions, although rebinding of PsbV and PsbU activated oxygen evolution in the absence of Cl− and Ca2+ ions in both the former and latter PSIIs. Based on these results, we proposed a model for the association of the five extrinsic proteins with intrinsic proteins in diatom PSII and compared it with those in PSIIs from the other organisms.
発行日
2010-09-17
出版物タイトル
The Journal of Biological Chemistry
285巻
38号
出版者
The American Society for Biochemistry and Molecular Biology, Inc.
開始ページ
29191
終了ページ
29199
ISSN
0021-9258
NCID
AA00251083
資料タイプ
学術雑誌論文
プロジェクト
エネルギー環境新素材拠点
オフィシャル URL
http://www.jbc.org/content/285/38/29191.abstract#aff-2
言語
English
著作権者
© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
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