ArticlePlant communications2025
Distinct features of PsbS essential for mediating plant photoprotection.
Article in Plant communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Probing the influence of PsbS on thylakoid lipid fluidity.Photosynthesis research · 2026Article
- pH-Dependent Vibrational Dynamics Drives Excited-State Quenching in the Phycobiliprotein Complex PC645.Journal of the American Chemical Society · 2026Article
- Chloroplasts and Plant Sustainability: Key Roles and Emerging Insights.International journal of molecular sciences · 2026Review
- CP26 is not involved in qE- or qZ-type non-photochemical quenching in Arabidopsis.Plant physiology · 2026Article
- Quantifying the Acidification-Induced Shift of the Dimerization Equilibrium of PsbS.The journal of physical chemistry letters · 2026Article
- Residue P132 of PsbS plays an important role in regulating the dynamics of non-photochemical quenching in Arabidopsis.Plant communications · 2026Article
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Identification of PsbS binding proteins inFrontiers in plant science · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
For optimum photosynthetic productivity, it is crucial for plants to swiftly transition between light-harvesting and photoprotective states as light conditions change in the field. The PsbS protein plays a pivotal role in this process by switching the light-harvesting antenna, light-harvesting complex II (LHCII), into the photoprotective state, energy-dependent chlorophyll fluorescence quenching (qE), to avoid photoinhibition in high-light environments. However, the molecular mechanism by which PsbS acts upon LHCII has remained unclear. In our study, we identified the specific amino acid domains that are essential for PsbS function. Using amino-acid point mutagenesis of PsbS in vivo, we found that the activation of photoprotection involves dynamic changes in the oligomeric state and conformation of PsbS, with two residues, E67 and E173, playing a key role in this process. Further, the replacement of hydrophobic phenylalanine residues in transmembrane helixes II (F83, F84, F87) and IV (F191, F193, F194) with tyrosine revealed that phenylalanine localized in helix IV can play a significant role in hydrophobic interactions of PsbS with LHCII. Removal of the 3
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.