ArticleThe Journal of biological chemistry2013
Mass spectrometry-based footprinting reveals structural dynamics of loop E of the chlorophyll-binding protein CP43 during photosystem II assembly in the cyanobacterium Synechocystis 6803.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed.
- Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the MnNature communications · 2026Article
- A Comment on "Deep Proteogenomics of a Photosynthetic Cyanobacterium".Journal of proteome research · 2026Article
- Structural interactions of TLP18.3 and Psb27-H1 to the luminal CP43 and rubredoxin-ENH1 to the stromal side of photosystem II in higher plants.The Journal of biological chemistry · 2026Article
- Structural comparison of allophycocyanin variants reveals the molecular basis for their spectral differences.Photosynthesis research · 2024Article
- Quality control in SARS-CoV-2 RBD-Fc vaccine production using LC-MS to confirm strain selection and detect contaminations from other strains.Scientific reports · 2024Article
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Binding and functions of the two chloride ions in the oxygen-evolving center of photosystem II.Photosynthesis research · 2022Review
- Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification.Photosynthesis research · 2022Article
- Properties of Photosystem II lacking the PsbJ subunit.Photosynthesis research · 2022Article
- 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
- Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.International journal of molecular sciences · 2022Review
- Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063.Nature plants · 2021Article
- 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
- The role of CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Revealing the architecture of protein complexes by an orthogonal approach combining HDXMS, CXMS, and disulfide trapping.Nature protocols · 2018Article
- Crystal structure of Psb27 from Arabidopsis thaliana determined at a resolution of 1.85 Å.Photosynthesis research · 2018Article
- Naphthylacetic Acid and Tea Polyphenol Application Promote Biomass and Lipid Production of Nervonic Acid-Producing Microalgae.Frontiers in plant science · 2018Article
- Reactive oxygen species leave a damage trail that reveals water channels in Photosystem II.Science advances · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The PSII repair cycle is required for sustainable photosynthesis in oxygenic photosynthetic organisms. In cyanobacteria and higher plants, proteolysis of the precursor D1 protein (pD1) to expose a C-terminal carboxylate group is an essential step leading to coordination of the Mn4CaO5 cluster, the site of water oxidation. Psb27 appears to associate with both pD1- and D1-containing PSII assembly intermediates by closely interacting with CP43. Here, we report that reduced binding affinity between CP43 and Psb27 is triggered by the removal of the C-terminal extension of the pD1 protein. A mass spectrometry-based footprinting strategy was adopted to probe solvent-exposed aspartic and glutamic acid residues on the CP43 protein. By comparing the extent of footprinting between HT3ΔctpAΔ27PSII and HT3ΔctpAPSII, two genetically modified PSII assembly complexes, we found that Psb27 binds to CP43 on the side of Loop E distal to the pseudo-symmetrical D1-D2 axis. By comparing a second pair of PSII assembly complexes, we discovered that Loop E of CP43 undergoes a significant conformational rearrangement due to the removal of the pD1 C-terminal extension, altering the Psb27-CP43 binding interface. The significance of this conformational rearrangement is discussed in the context of recruitment of the PSII lumenal extrinsic proteins and Mn4CaO5 cluster assembly. In addition to CP43's previously known function as one of the core PSII antenna proteins, this work demonstrates that Loop E of CP43 plays an important role in the functional assembly of the Water Oxidizing Center (WOC) during PSII biogenesis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.