ArticlePhotosynthesis research2014
Crystal structure of CyanoQ from the thermophilic cyanobacterium Thermosynechococcus elongatus and detection in isolated photosystem II complexes.
Article in Photosynthesis research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the MnNature communications · 2026Article
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- The lumenal domain of Cyt bPhotosynthesis research · 2025Article
- The biogenesis and maintenance of PSII: Recent advances and current challenges.The Plant cell · 2024Review
- Evolutionary diversity of proton and water channels on the oxidizing side of photosystem II and their relevance to function.Photosynthesis research · 2023Review
- 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
- Structural insights into photosystem II assembly.Nature plants · 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
- Crystal Structure of Geranylgeranyl Pyrophosphate Synthase (CrtE) Involved in Cyanobacterial Terpenoid Biosynthesis.Frontiers in plant science · 2020Article
- Comparison of photosynthetic performances of marine picocyanobacteria with different configurations of the oxygen-evolving complex.Photosynthesis research · 2018Article
- Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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
- Identification and Roles of Photosystem II Assembly, Stability, and Repair Factors in Arabidopsis.Frontiers in plant science · 2016Review
- Article
- Characterization of a Synechocystis sp. PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II.Photosynthesis research · 2015Article
- Article
- Enhancing the production of chlorophyll f in the cyanobacterium Synechocystis sp. PCC 6803.Physiologia plantarumArticle
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8 authors.
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Abstract
The PsbQ-like protein, termed CyanoQ, found in the cyanobacterium Synechocystis sp. PCC 6803 is thought to bind to the lumenal surface of photosystem II (PSII), helping to shield the Mn4CaO5 oxygen-evolving cluster. CyanoQ is, however, absent from the crystal structures of PSII isolated from thermophilic cyanobacteria raising the possibility that the association of CyanoQ with PSII might not be a conserved feature. Here, we show that CyanoQ (encoded by tll2057) is indeed expressed in the thermophilic cyanobacterium Thermosynechococcus elongatus and provide evidence in support of its assignment as a lipoprotein. Using an immunochemical approach, we show that CyanoQ co-purifies with PSII and is actually present in highly pure PSII samples used to generate PSII crystals. The absence of CyanoQ in the final crystal structure is possibly due to detachment of CyanoQ during crystallisation or its presence in sub-stoichiometric amounts. In contrast, the PsbP homologue, CyanoP, is severely depleted in isolated PSII complexes. We have also determined the crystal structure of CyanoQ from T. elongatus to a resolution of 1.6 Å. It lacks bound metal ions and contains a four-helix up-down bundle similar to the ones found in Synechocystis CyanoQ and spinach PsbQ. However, the N-terminal region and extensive lysine patch that are thought to be important for binding of PsbQ to PSII are not conserved in T. elongatus CyanoQ.
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