ArticlePhotosynthesis research2015
Multiple copies of the PsbQ protein in a cyanobacterial photosystem II assembly intermediate complex.
Article in Photosynthesis research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Simultaneous acclimation to nitrogen and iron scarcity in open ocean cyanobacteria revealed by sparse tensor decomposition of metatranscriptomes.Science advances · 2025Article
- Comparison of PsbQ and Psb27 in photosystem II provides insight into their roles.Photosynthesis research · 2022Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- Structural Coupling of Extrinsic Proteins with the Oxygen-Evolving Center in Photosystem II.Frontiers in plant science · 2016Review
- The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.Frontiers in plant science · 2016Review
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosystem II (PSII) undergoes frequent damage owing to the demanding electron transfer chemistry it performs. To sustain photosynthetic activity, damaged PSII undergoes a complex repair cycle consisting of many transient intermediate complexes. By purifying PSII from the cyanobacterium Synechocystis sp. PCC 6803 using a histidine-tag on the PsbQ protein, a lumenal extrinsic subunit, a novel PSII assembly intermediate was isolated in addition to the mature PSII complex. This new complex, which we refer to as PSII-Q4, contained four copies of the PsbQ protein per PSII monomer, instead of the expected one copy. In addition, PSII-Q4 lacked two other lumenal extrinsic proteins, PsbU and PsbV, which are present in the mature PSII complex. We suggest that PSII-Q4 is a late PSII assembly intermediate that is formed just before the binding of PsbU and PsbV, and we incorporate these results into an updated model of PSII assembly.
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Registered trials
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