Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii
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Abstract
Photosystem II (PSII) catalyzes water oxidation and plastoquinone reduction by utilizing light energy. It is highly susceptible to photodamage under high-light conditions and the damaged PSII needs to be restored through a process known as the PSII repair cycle. The detailed molecular mechanism underlying the PSII repair process remains mostly elusive. Here, we report biochemical and structural features of a PSII-repair intermediate complex, likely arrested at an early stage of the PSII repair process in the green alga Chlamydomonas reinhardtii . The complex contains three protein factors associated with a damaged PSII core, namely Thylakoid Enriched Factor 14 (TEF14), Photosystem II Repair Factor 1 (PRF1), and Photosystem II Repair Factor 2 (PRF2). TEF14, PRF1 and PRF2 may facilitate the release of the manganese-stabilizing protein PsbO, disassembly of peripheral light-harvesting complexes from PSII and blockage of the Q B site, respectively. Moreover, an α-tocopherol quinone molecule is located adjacent to the heme group of cytochrome b 559 , potentially fulfilling a photoprotective role by preventing the generation of reactive oxygen species.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
TIM, a targeted insertional mutagenesis method utilizing CRISPR/Cas9 in Chlamydomonas reinhardtii
Picariello, T., Hou, Y., Kubo, T., McNeill, N. A., Yanagisawa, H.-A., Oda, T., & Witman, G. B. (2020) · PLOS ONE · doi:10.1371/journal.pone.0232594 · Cited by 83 · see citing works
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- Authors
- Li, A., You, T., Pang, X., Wang, Y., Tian, L., Li, X., & Liu, Z.
- Affiliations
- Chinese Academy of Sciences (CN)
- Westlake University (CN)
- Corresponding author
- Li, Xiaobo
- Liu, Zhenfeng
- Venue
- Nature Communications
- Published
- 2024-06-18
- Volume
- 15
- Issue
- 1
- Pages
- 5211-5211
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11189392
- OpenAlex
- W4399766566
- Cited by
- 26
- References
- 2
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 3
- FWCI
- 3.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (32170255, 31925024, YSBR-015)
- Chinese Academy of Sciences (XDB37020101, XDB27020106, YSBR‐015)
- Institute of Biophysics, Chinese Academy of Sciences
- Natural Science Foundation of Zhejiang Province
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Keywords
- photosystem II repair, Chlamydomonas reinhardtii, PRF1, PsbO, manganese-stabilizing protein, QB site, cytochrome b559, photoprotection, reactive oxygen species, photodamage, protein structure
- MeSH terms
- Cytochrome b Group, Light, Oxidation-Reduction, Plant Proteins, Chlamydomonas reinhardtii, Reactive Oxygen Species, Thylakoids, Photosystem II Protein Complex, Light-Harvesting Protein Complexes
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