Evidence map›Paper›PMID 27183269›Full record

ArticleeLife2016

Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation.

William John Allen, Robin Adam Corey, Peter Oatley, Richard Barry Sessions, Steve A Baldwin, Sheena E Radford, Roman Tuma, Ian Collinson

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. The Multifunctional Preprotein Binding Domain of SecA.Chembiochem : a European journal of chemical biology · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. DynamicsProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  18. Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

William John AllenSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-9513-4786
Robin Adam CoreySchool of Biochemistry, University of Bristol, Bristol, United Kingdom.
Peter OatleyAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Richard Barry SessionsSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.
Steve A BaldwinAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Sheena E RadfordAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-3079-8039
Roman TumaAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Ian CollinsonSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-3931-0503

Funding

Biotechnology and Biological Sciences Research Council BB/I006737/1Biotechnology and Biological Sciences Research Council BB/I008675/1Biotechnology and Biological Sciences Research Council BB/M003604/1European Research Council 322408Wellcome TrustWellcome Trust 104632
6 · The paper itself

Abstract

The essential process of protein secretion is achieved by the ubiquitous Sec machinery. In prokaryotes, the drive for translocation comes from ATP hydrolysis by the cytosolic motor-protein SecA, in concert with the proton motive force (PMF). However, the mechanism through which ATP hydrolysis by SecA is coupled to directional movement through SecYEG is unclear. Here, we combine all-atom molecular dynamics (MD) simulations with single molecule FRET and biochemical assays. We show that ATP binding by SecA causes opening of the SecY-channel at long range, while substrates at the SecY-channel entrance feed back to regulate nucleotide exchange by SecA. This two-way communication suggests a new, unifying 'Brownian ratchet' mechanism, whereby ATP binding and hydrolysis bias the direction of polypeptide diffusion. The model represents a solution to the problem of transporting inherently variable substrates such as polypeptides, and may underlie mechanisms of other motors that translocate proteins and nucleic acids.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid MotifsBacterial ProteinsBinding SitesEscherichia coliGene ExpressionKineticsMethanocaldococcusModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein TransportRecombinant ProteinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsRecombinant ProteinsSecA ProteinsSEC Translocation ChannelsbiochemistrybiophysicsE. colimolecular dynamicsprotein secretionprotein translocationSecASecYEGsingle molecule FRETstructural biology

Identifiers

PMID27183269
PMCPMC4907695

What OpenQuestion holds

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LicenceCC BY
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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.