ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 78 citations in OpenAlex.
- Article
- Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the MnNature communications · 2026Article
- On the non-oxygenic origins of thylakoids.Communications biology · 2025Review
- Complexome profiling of the Chlamydomonas psb28 mutant reveals TEF5 as an early PSII assembly factor.The Plant cell · 2025Article
- Adaptive responses of plants to light stress: mechanisms of photoprotection and acclimation. A review.Frontiers in plant science · 2025Review
- The biogenesis and maintenance of PSII: Recent advances and current challenges.The Plant cell · 2024Review
- Indirect interactions involving the PsbM or PsbT subunits and the PsbO, PsbU and PsbV proteins stabilize assembly and activity of Photosystem II in Synechocystis sp. PCC 6803.Photosynthesis research · 2024Article
- The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis.Nature communications · 2023Article
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- Photosynthetic efficiency and transcriptome analysis ofFrontiers in plant science · 2023Article
- Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins.Plant physiology · 2022Article
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
- Complexome profiling on the Chlamydomonas lpa2 mutant reveals insights into PSII biogenesis and new PSII associated proteins.Journal of experimental botany · 2022Article
- Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063.Nature plants · 2021Article
- Probing the biogenesis pathway and dynamics of thylakoid membranes.Nature communications · 2021Article
- Purification of Protein-complexes from the CyanobacteriumBio-protocol · 2020Article
- ONE-HELIX PROTEIN1 and 2 Form Heterodimers to Bind Chlorophyll in Photosystem II Biogenesis.Plant physiology · 2020Article
- A novel chlorophyll protein complex in the repair cycle of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Photosynthesis-Specific Rubredoxin-Like Protein Is Required for Efficient Association of the D1 and D2 Proteins during the Initial Steps of Photosystem II Assembly.The Plant cell · 2019Article
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8 authors at 4 institutions in 3 countries.
Funding
Abstract
Photosystem II (PSII) mutants are useful experimental tools to trap potential intermediates involved in the assembly of the oxygen-evolving PSII complex. Here, we focus on the subunit composition of the RC47 assembly complex that accumulates in a psbC null mutant of the cyanobacterium Synechocystis sp. PCC 6803 unable to make the CP43 apopolypeptide. By using native gel electrophoresis, we showed that RC47 is heterogeneous and mainly found as a monomer of 220 kDa. RC47 complexes co-purify with small Cab-like proteins (ScpC and/or ScpD) and with Psb28 and its homologue Psb28-2. Analysis of isolated His-tagged RC47 indicated the presence of D1, D2, the CP47 apopolypeptide, plus nine of the 13 low-molecular-mass (LMM) subunits found in the PSII holoenzyme, including PsbL, PsbM and PsbT, which lie at the interface between the two momomers in the dimeric holoenzyme. Not detected were the LMM subunits (PsbK, PsbZ, Psb30 and PsbJ) located in the vicinity of CP43 in the holoenzyme. The photochemical activity of isolated RC47-His complexes, including the rate of reduction of P680(+), was similar to that of PSII complexes lacking the Mn(4)CaO(5) cluster. The implications of our results for the assembly and repair of PSII in vivo are discussed.
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