ArticleThe Journal of biological chemistry2008
Interactions between the photosystem II subunit PsbS and xanthophylls studied in vivo and in vitro.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 149 citations in OpenAlex.
- Nonphotochemical quenching in plants: Mechanisms and mysteries.The Plant cell · 2025Review
- Photoautotrophic cultivation of a Chlamydomonas reinhardtii mutant with zeaxanthin as the sole xanthophyll.Biotechnology for biofuels and bioproducts · 2024Article
- The Photoprotective Protein PsbS from Green MicroalgaInternational journal of molecular sciences · 2023Article
- The Geomagnetic Field (GMF) Is Required for Lima Bean Photosynthesis and Reactive Oxygen Species Production.International journal of molecular sciences · 2023Article
- pH-Dependent Conformational Switch Impacts Stability of the PsbS Dimer.The journal of physical chemistry letters · 2023Article
- High light-induced changes in whole-cell proteomic profile and its correlation with the organization of thylakoid super-complex in cyclic electron transport mutants ofFrontiers in plant science · 2023Article
- Transcriptional regulation of photoprotection in dark-to-light transition-More than just a matter of excess light energy.Science advances · 2022Article
- Biochemical and molecular properties of LHCX1, the essential regulator of dynamic photoprotection in diatoms.Plant physiology · 2022Article
- Light-induced HY5 Functions as a Systemic Signal to Coordinate the Photoprotective Response to Light Fluctuation.Plant physiology · 2020Article
- Rapid regulation of photosynthetic light harvesting in the absence of minor antenna and reaction centre complexes.Journal of experimental botany · 2020Article
- Light-harvesting complexes access analogue emissive states in different environments.Chemical science · 2020Article
- On the PsbS-induced quenching in the plant major light-harvesting complex LHCII studied in proteoliposomes.Photosynthesis research · 2020Article
- Photoprotection and growth under different lights of Arabidopsis single and double mutants for energy dissipation (npq4) and state transitions (pph1).Plant cell reports · 2019Article
- Molecular Anatomy of Plant Photoprotective Switches: The Sensitivity of PsbS to the Environment, Residue by Residue.The journal of physical chemistry letters · 2019Article
- The Low Molecular Mass Photosystem II Protein PsbTn Is Important for Light Acclimation.Plant physiology · 2019Article
- A New Light on Photosystem II Maintenance in Oxygenic Photosynthesis.Frontiers in plant science · 2019Review
- The Photosystem II Subunit S under Stress.Biophysical journal · 2017Article
- Large-scale in vitro production, refolding and dimerization of PsbS in different microenvironments.Scientific reports · 2017Article
- A Light Harvesting Complex-Like Protein in Maintenance of Photosynthetic Components inPlant physiology · 2017Article
- Depth-specific fluctuations of gene expression and protein abundance modulate the photophysiology in the seagrass Posidonia oceanica.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The photosystem II subunit PsbS is essential for excess energy dissipation (qE); however, both lutein and zeaxanthin are needed for its full activation. Based on previous work, two models can be proposed in which PsbS is either 1) the gene product where the quenching activity is located or 2) a proton-sensing trigger that activates the quencher molecules. The first hypothesis requires xanthophyll binding to two PsbS-binding sites, each activated by the protonation of a dicyclohexylcarbodiimide-binding lumen-exposed glutamic acid residue. To assess the existence and properties of these xanthophyll-binding sites, PsbS point mutants on each of the two Glu residues PsbS E122Q and PsbS E226Q were crossed with the npq1/npq4 and lut2/npq4 mutants lacking zeaxanthin and lutein, respectively. Double mutants E122Q/npq1 and E226Q/npq1 had no qE, whereas E122Q/lut2 and E226Q/lut2 showed a strong qE reduction with respect to both lut2 and single glutamate mutants. These findings exclude a specific interaction between lutein or zeaxanthin and a dicyclohexylcarbodiimide-binding site and suggest that the dependence of nonphotochemical quenching on xanthophyll composition is not due to pigment binding to PsbS. To verify, in vitro, the capacity of xanthophylls to bind PsbS, we have produced recombinant PsbS refolded with purified pigments and shown that Raman signals, previously attributed to PsbS-zeaxanthin interactions, are in fact due to xanthophyll aggregation. We conclude that the xanthophyll dependence of qE is not due to PsbS but to other pigment-binding proteins, probably of the Lhcb type.
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