ArticleProceedings of the National Academy of Sciences of the United States of America2007
The PsbQ protein defines cyanobacterial Photosystem II complexes with highest activity and stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 91 citations in OpenAlex.
- Harnessing salinity induced adaptive potential of extracellular polymeric substances producing rice-field cyanobacterium Neowestiellopsis sp. VKB03: a physiochemical, morphological, and biomass characterization.World journal of microbiology & biotechnology · 2026Article
- The NSvc4 Protein of Rice Stripe Virus Suppresses Chloroplast-Mediated Defense by Interacting with NbPsbQ.International journal of molecular sciences · 2026Article
- Spatial proteomics reveals signal sequence characteristics correlated with localization in cyanobacteria.Plant physiology · 2025Article
- Article
- Light-dependent signal transduction in the marine diatomProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Binding and functions of the two chloride ions in the oxygen-evolving center of photosystem II.Photosynthesis research · 2022Review
- Comparison of PsbQ and Psb27 in photosystem II provides insight into their roles.Photosynthesis research · 2022Article
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
- 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
- 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
- Proximity-based proteomics reveals the thylakoid lumen proteome in the cyanobacterium Synechococcus sp. PCC 7002.Photosynthesis research · 2021Article
- Comparison of photosynthetic performances of marine picocyanobacteria with different configurations of the oxygen-evolving complex.Photosynthesis research · 2018Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- 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
- Multiple copies of the PsbQ protein in a cyanobacterial photosystem II assembly intermediate complex.Photosynthesis research · 2015Article
- Crystal structure of CyanoQ from the thermophilic cyanobacterium Thermosynechococcus elongatus and detection in isolated photosystem II complexes.Photosynthesis research · 2014Article
- MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mass spectroscopy locates the extrinsic proteins of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Localization of the CyanoP binding site on photosystem II by surface plasmon resonance spectroscopy.Frontiers in plant science · 2014Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Light-induced conversion of water to molecular oxygen by Photosystem II (PSII) is one of the most important enzymatic reactions in the biosphere. PSII is a multisubunit membrane protein complex with numerous associated cofactors, but it continually undergoes assembly and disassembly due to frequent light-mediated damage as a result of its normal function. Thus, at any instant, there is heterogeneity in the subunit compositions of PSII complexes within the cell. In particular, cyanobacterial PSII complexes have five associated extrinsic proteins, PsbO, PsbP, PsbQ, PsbU, and PsbV. However, little is known about the interactions of the more recently identified PsbQ protein with other components in cyanobacterial PSII. Here we show that PSII complexes can be isolated from the cyanobacterium Synechocystis sp. PCC 6803 on the basis of the presence of a polyhistidine-tagged PsbQ protein. Purification of PSII complexes using a tagged extrinsic protein has not been previously described, and this work conclusively demonstrates that PsbQ is present in combination with the PsbO, PsbU, and PsbV proteins in cyanobacterial PSII. Moreover, PsbQ-associated PSII complexes have higher activity and stability relative to those isolated using histidine-tagged CP47, an integral membrane protein. Therefore, we conclude that the presence of PsbQ defines the fully assembled and optimally active form of the enzyme.
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