ArticleThe Journal of biological chemistry2014
Cross-linking evidence for multiple interactions of the PsbP and PsbQ proteins in a higher plant photosystem II supercomplex.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- The NSvc4 Protein of Rice Stripe Virus Suppresses Chloroplast-Mediated Defense by Interacting with NbPsbQ.International journal of molecular sciences · 2026Article
- Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance.Nature communications · 2026Article
- The lumenal domain of Cyt bPhotosynthesis research · 2025Article
- Nonpigmented PsbR is involved in the integrity of excitation landscape in higher plant photosystem II, a case study in Arabidopsis thaliana and a mutant.Photosynthesis research · 2025Article
- Protein phosphorylation and oxidative protein modification promote plant photosystem II disassembly for repair.Plant communications · 2025Article
- Architecture and functional regulation of a plant PSII-LHCII megacomplex.Science advances · 2024Article
- Effects of abiotic stress on photosystem II proteins.Photosynthetica · 2023Review
- Single-molecule real-time sequencing of the full-length transcriptome of Halophila beccarii.Scientific reports · 2022Article
- Binding and functions of the two chloride ions in the oxygen-evolving center of photosystem II.Photosynthesis research · 2022Review
- Macromolecular conformational changes in photosystem II: interaction between structure and function.Biophysical reviews · 2022Review
- Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium.Nature communications · 2022Article
- Molecular Mechanisms Underlying the Acclimation ofFrontiers in plant science · 2021Article
- Cloning and characterization of two chlorophyll A/B binding protein genes and analysis of their gene family in Camellia sinensis.Scientific reports · 2020Article
- Light-dependent N-terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii.The Plant journal : for cell and molecular biology · 2019Article
- Elevated COBMC plant biology · 2019Article
- Photosystem II Extrinsic Proteins and Their Putative Role in Abiotic Stress Tolerance in Higher Plants.Plants (Basel, Switzerland) · 2018Review
- In vivo system for analyzing the function of the PsbP protein using Chlamydomonas reinhardtii.Photosynthesis research · 2017Article
- Structurally conserved channels in cyanobacterial and plant photosystem II.Photosynthesis research · 2017Article
- Isolation of novel PSII-LHCII megacomplexes from pea plants characterized by a combination of proteomics and electron microscopy.Photosynthesis research · 2016Article
- Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extrinsic subunits of membrane-bound photosystem II (PSII) maintain an essential role in optimizing the water-splitting reaction of the oxygen-evolving complex (OEC), even though they have undergone drastic change during the evolution of oxyphototrophs from symbiotic cyanobacteria to chloroplasts. Two specific extrinsic proteins, PsbP and PsbQ, bind to the lumenal surface of PSII in green plants and maintain OEC conformation and stabilize overall enzymatic function; however, their precise location has not been fully resolved. In this study, PSII-enriched membranes, isolated from spinach, were subjected to chemical cross-linking combined with release-reconstitution experiments. We observed direct interactions between PsbP and PsbE, as well as with PsbR. Intriguingly, PsbP and PsbQ were further linked to the CP26 and CP43 light-harvesting proteins. In addition, two cross-linked sites, between PsbP and PsbR, and that of PsbP and CP26, were identified by tandem mass spectrometry. These data were used to estimate the binding topology and location of PsbP, and the putative positioning of PsbQ and PsbR on the lumenal surface of the PSII. Our model gives new insights into the organization of PSII extrinsic subunits in higher plants and their function in stabilizing the OEC of the PSII supercomplex.
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