Evidence map›Paper›PMID 21056980›Full record

ArticleThe Journal of biological chemistry2011

The oligomeric state and arrangement of the active bacterial translocon.

Karine Deville, Vicki A M Gold, Alice Robson, Sarah Whitehouse, Richard B Sessions, Stephen A Baldwin, Sheena E Radford, Ian Collinson

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. SecA-a New Twist in the Tale.Journal of bacteriology · 2017
    Article
  14. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  15. Article
  16. Article
  17. Unlocking the Bacterial SecY Translocon.Structure (London, England : 1993) · 2016
    Article
  18. Article
  19. Channel crossing: how are proteins shipped across the bacterial plasma membrane?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  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.

Karine DevilleAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Vicki A M Gold
Alice Robson
Sarah Whitehouse
Richard B Sessions
Stephen A Baldwin
Sheena E Radford
Ian Collinson

Funding

Biotechnology and Biological Sciences Research Council BB/F002343/1Wellcome TrustWellcome Trust 080705/Z/06/ZWellcome Trust 082140Wellcome Trust 084452
6 · The paper itself

Abstract

Protein secretion in bacteria is driven through the ubiquitous SecYEG complex by the ATPase SecA. The structure of SecYEG alone or as a complex with SecA in detergent reveal a monomeric heterotrimer enclosing a central protein channel, yet in membranes it is dimeric. We have addressed the functional significance of the oligomeric status of SecYEG in protein translocation using single molecule and ensemble methods. The results show that while monomers are sufficient for the SecA- and ATP-dependent association of SecYEG with pre-protein, active transport requires SecYEG dimers arranged in the back-to-back conformation. Molecular modeling of this dimeric structure, in conjunction with the new functional data, provides a rationale for the presence of both active and passive copies of SecYEG in the functional translocon.

Indexed as

Models, MolecularAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsProtein MultimerizationProtein TransportSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsSecA ProteinsSEC Translocation Channels

Identifiers

PMID21056980
PMCPMC3039378

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.