ID | 66496 |
フルテキストURL | |
著者 |
Kato, Yusuke
Institute of Plant Science and Resources (IPSR), Okayama University
Kuroda, Hiroshi
Research Institute for Interdisciplinary Science, Okayama University
Ozawa, Shin-Ichiro
Institute of Plant Science and Resources (IPSR), Okayama University
Saito, Keisuke
Research Center for Advanced Science and Technology, The University of Tokyo
Dogra, Vivek
Shanghai Center for Plant Stress Biology, Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences
Scholz, Martin
Institute of Plant Biology and Biotechnology, University of Münster
Zhang, Guoxian
Institute of Plant Science and Resources (IPSR), Okayama University
de Vitry, Catherine
Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, Centre National de la Recherche Scientifique and Sorbonne Université Pierre et Marie Curie
Ishikita, Hiroshi
Research Center for Advanced Science and Technology, The University of Tokyo
Kim, Chanhong
Shanghai Center for Plant Stress Biology, Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences
Hippler, Michael
Institute of Plant Science and Resources (IPSR), Okayama University
Takahashi, Yuichiro
Research Institute for Interdisciplinary Science, Okayama University
ORCID
Kaken ID
publons
researchmap
Sakamoto, Wataru
Institute of Plant Science and Resources (IPSR), Okayama University
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抄録 | Photosynthesis is one of the most important reactions for sustaining our environment. Photosystem II (PSII) is the initial site of photosynthetic electron transfer by water oxidation. Light in excess, however, causes the simultaneous production of reactive oxygen species (ROS), leading to photo-oxidative damage in PSII. To maintain photosynthetic activity, the PSII reaction center protein D1, which is the primary target of unavoidable photo-oxidative damage, is efficiently degraded by FtsH protease. In PSII subunits, photo-oxidative modifications of several amino acids such as Trp have been indeed documented, whereas the linkage between such modifications and D1 degradation remains elusive. Here, we show that an oxidative post-translational modification of Trp residue at the N-terminal tail of D1 is correlated with D1 degradation by FtsH during high-light stress. We revealed that Arabidopsis mutant lacking FtsH2 had increased levels of oxidative Trp residues in D1, among which an N-terminal Trp-14 was distinctively localized in the stromal side. Further characterization of Trp-14 using chloroplast transformation in Chlamydomonas indicated that substitution of D1 Trp-14 to Phe, mimicking Trp oxidation enhanced FtsH-mediated D1 degradation under high light, although the substitution did not affect protein stability and PSII activity. Molecular dynamics simulation of PSII implies that both Trp-14 oxidation and Phe substitution cause fluctuation of D1 N-terminal tail. Furthermore, Trp-14 to Phe modification appeared to have an additive effect in the interaction between FtsH and PSII core in vivo. Together, our results suggest that the Trp oxidation at its N-terminus of D1 may be one of the key oxidations in the PSII repair, leading to processive degradation by FtsH.
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キーワード | post-translational modification
Arabidopsis thaliana
protein degradation
photosystem II
photo-oxidative damage
tryptophan oxidation
Chlamydomonas reinhardtii
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発行日 | 2023-11-21
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出版物タイトル |
eLife
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巻 | 12巻
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出版者 | eLife Sciences Publications
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開始ページ | RP88822
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ISSN | 2050-084X
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資料タイプ |
学術雑誌論文
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言語 |
英語
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OAI-PMH Set |
岡山大学
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著作権者 | © Kato, Kuroda, Ozawa et al.
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論文のバージョン | publisher
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
関連URL | isVersionOf https://doi.org/10.7554/eLife.88822
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ライセンス | https://creativecommons.org/licenses/by/4.0/
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Citation | Yusuke Kato, Hiroshi Kuroda, Shin-Ichiro Ozawa, Keisuke Saito, Vivek Dogra, Martin Scholz, Guoxian Zhang, Catherine de Vitry, Hiroshi Ishikita, Chanhong Kim, Michael Hippler, Yuichiro Takahashi, Wataru Sakamoto (2023) Characterization of tryptophan oxidation affecting D1 degradation by FtsH in the photosystem II quality control of chloroplasts eLife 12:RP88822.
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助成機関名 |
Ministry of Education, Culture, Sports, Science and Technology
Japan Society for the Promotion of Science
Oohara Foundation
Sorbonne Université
Agence Nationale de la Recherche
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助成番号 | 23H04959
21H02508
21K06221
23H04963
UMR7141
ANR-11-LABX-0011-01
20H03217
23H02444
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