Characterization of tryptophan oxidation affecting D1 degradation by FtsH in the photosystem II quality control of chloroplasts
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Abstract
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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- Authors
- Kato, Y., Kuroda, H., Ozawa, S.-I., Saito, K., Dogra, V., Scholz, M., Zhang, G., de Vitry, C., Ishikita, H., Kim, C., Hippler, M., Takahashi, Y., & Sakamoto, W.
- Affiliations
- Setsunan University (JP)
- Okayama University (JP)
- Research Center for Advanced Science and Technology, The University of Tokyo (JP)
- Chinese Academy of Sciences (CN)
- University of Münster (DE)
- Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, Centre National de la Recherche Scientifique and Sorbonne Université Pierre et Marie Curie
- ORCID
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2023-11-21
- Volume
- 12
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W4388848710
- Cited by
- 26
- References
- 75
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 11
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology (KAKENHI (23H04959), KAKENHI (23H04963))
- Japan Society for the Promotion of Science (KAKENHI (21H02508), KAKENHI (21K06221), KAKENHI (20H03217), KAKENHI (23H02444))
- Oohara Foundation
- Sorbonne Université (UMR7141)
- Agence Nationale de la Recherche (ANR-11-LABX-0011-01)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- tryptophan oxidation, photosystem II, D1 protein degradation, FtsH protease, high light stress, photooxidative damage, N-terminal tail, post-translational modification, protein quality control, chloroplasts, Arabidopsis, Chlamydomonas, molecular dynamics simulation, protein stability
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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