ArticleProceedings of the National Academy of Sciences of the United States of America2014
MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 48 citations in OpenAlex.
- Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the MnNature communications · 2026Article
- Comparison of PsbQ and Psb27 in photosystem II provides insight into their roles.Photosynthesis research · 2022Article
- High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium,Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Comparative genomic analysis of the aldehyde dehydrogenase gene superfamily inFrontiers in plant science · 2022Article
- The Photosystem II Assembly Factor Ycf48 from the CyanobacteriumInternational journal of molecular sciences · 2021Article
- Structural insights into a dimeric Psb27-photosystem II complex from a cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- iTRAQ-Based Comparative Proteomic Analysis Provides Insights into Molecular Mechanisms of Salt Tolerance in Sugar Beet (International journal of molecular sciences · 2018Article
- Chemical cross-linking in the structural analysis of protein assemblies.Methods (San Diego, Calif.) · 2018Review
- Development of Large-scale Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2018Article
- Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Chloramphenicol acetyltransferase-a new selectable marker in stable nuclear transformation of the red alga Cyanidioschyzon merolae.Protoplasma · 2017Article
- A Novel Redoxin in the Thylakoid Membrane Regulates the Titer of Photosystem I.The Journal of biological chemistry · 2016Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga.The Journal of biological chemistry · 2016Article
- Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation.Biochemistry · 2016Article
- The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.Frontiers in plant science · 2016Review
- Structural Coupling of Extrinsic Proteins with the Oxygen-Evolving Center in Photosystem II.Frontiers in plant science · 2016Review
- Environmental pH and the Requirement for the Extrinsic Proteins of Photosystem II in the Function of Cyanobacterial Photosynthesis.Frontiers in plant science · 2016Article
- Multiple copies of the PsbQ protein in a cyanobacterial photosystem II assembly intermediate complex.Photosynthesis research · 2015Article
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6 authors at 1 institution in 1 country.
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Abstract
PsbQ is a luminal extrinsic protein component that regulates the water splitting activity of photosystem II (PSII) in plants, algae, and cyanobacteria. However, PsbQ is not observed in the currently available crystal structures of PSII from thermophilic cyanobacteria. The structural location of PsbQ within the PSII complex has therefore remained unknown. Here, we report chemical cross-linking followed by immunodetection and liquid chromatography/tandem MS analysis of a dimeric PSII complex isolated from the model cyanobacterium, Synechocystis sp. PCC 6803, to determine the binding site of PsbQ within PSII. Our results demonstrate that PsbQ is closely associated with the PsbO and CP47 proteins, as revealed by cross-links detected between (120)K of PsbQ and (180)K and (59)K of PsbO, and between (102)K of PsbQ and (440)D of CP47. We further show that genetic deletion of the psbO gene results in the complete absence of PsbQ in PSII complexes as well as the loss of the dimeric form of PSII. Overall, our data provide a molecular-level description of the enigmatic binding site of PsbQ in PSII in a cyanobacterium. These results also help us understand the sequential incorporation of the PsbQ protein during the PSII assembly process, as well as its stabilizing effect on the oxygen evolution activity of PSII.
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