Evidence map›Paper›PMID 22991268›Full record

ArticleThe Plant cell2012

Subunit organization of a synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair.

Marko Boehm, Jianfeng Yu, Vendula Krynicka, Myles Barker, Martin Tichy, Josef Komenda, Peter J Nixon, Jon Nield

Abstract read
In one paragraph

Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed.

  1. Article
  2. Article
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  4. Regulation of mixotrophy inMicrobiology (Reading, England) · 2026
    Article
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Silencing of PepperInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022
    Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Marko BoehmDivision of Molecular Biosciences, Imperial College London, London SW7 2AZ, United Kingdom.
Jianfeng Yu
Vendula Krynicka
Myles Barker
Martin Tichy
Josef Komenda
Peter J Nixon
Jon Nield

Funding

Biotechnology and Biological Sciences Research Council BB/F020554/1Biotechnology and Biological Sciences Research Council BB/F021526/1
6 · The paper itself

Abstract

FtsH metalloproteases are key components of the photosystem II (PSII) repair cycle, which operates to maintain photosynthetic activity in the light. Despite their physiological importance, the structure and subunit composition of thylakoid FtsH complexes remain uncertain. Mutagenesis has previously revealed that the four FtsH homologs encoded by the cyanobacterium Synechocystis sp PCC 6803 are functionally different: FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. To gain insights into FtsH2, which is involved in selective D1 protein degradation during PSII repair, we used a strain of Synechocystis 6803 expressing a glutathione S-transferase (GST)-tagged derivative (FtsH2-GST) to isolate FtsH2-containing complexes. Biochemical analysis revealed that FtsH2-GST forms a hetero-oligomeric complex with FtsH3. FtsH2 also interacts with FtsH3 in the wild-type strain, and a mutant depleted in FtsH3, like ftsH2(-) mutants, displays impaired D1 degradation. FtsH3 also forms a separate heterocomplex with FtsH1, thus explaining why FtsH3 is more important than FtsH2 for cell viability. We investigated the structure of the isolated FtsH2-GST/FtsH3 complex using transmission electron microscopy and single-particle analysis. The three-dimensional structural model obtained at a resolution of 26 Å revealed that the complex is hexameric and consists of alternating FtsH2/FtsH3 subunits.

Indexed as

Models, MolecularGlutathione TransferaseLightMetalloproteasesMicroscopy, Electron, TransmissionMultienzyme ComplexesMutationNegative StainingOxygenPhenotypePhotosystem II Protein ComplexProtein Interaction MappingProteolysisRecombinant Fusion ProteinsSequence Analysis, ProteinSynechocystisGlutathione TransferaseMetalloproteasesMultienzyme ComplexesOxygenPhotosystem II Protein ComplexRecombinant Fusion Proteins

Identifiers

PMID22991268
PMCPMC3480294

What OpenQuestion holds

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Registered trials

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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.