Evidence map›Paper›PMID 22074917›Full record

ArticleThe Journal of biological chemistry2012

Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.

Kazuhiro Morita, Hajime Tokuda, Ken-Ichi Nishiyama

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. 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
  3. Article
  4. The Structure ofInternational journal of molecular sciences · 2020
    Article
  5. Direct visualization of theScience advances · 2019
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. 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

3 authors.

Kazuhiro MoritaInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Hajime TokudaInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Ken-Ichi NishiyamaInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan. Electronic address: nishiyam@iwate-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SecA is a translocation ATPase that drives protein translocation. D209N SecA, a dominant-negative mutant, binds ATP but is unable to hydrolyze it. This mutant was inactive to proOmpA translocation. However, it generated a translocation intermediate of 18 kDa. Further addition of wild-type SecA caused its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation caused a topology inversion of SecG. Moreover, an intermediate of SecG inversion was identified when wild-type and D209N SecA were used in the same amounts. These results indicate that multiple SecA molecules drive translocation across a single translocon with SecG inversion. Here, we propose a revised model of proOmpA translocation in which a single catalytic cycle of SecA causes translocation of 10-13 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid MotifsBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coliEscherichia coli ProteinsHydrolysisMembrane ProteinsMembrane Transport ProteinsMutationProtein PrecursorsProtein StabilityProtein Structure, TertiaryProtein TransportSecA ProteinsAdenosine TriphosphatasesAdenosine TriphosphateBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsOMPA outer membrane proteinsProtein PrecursorsSecA ProteinsSecG protein, E coliSEC Translocation Channels

Identifiers

PMID22074917
PMCPMC3249098

What OpenQuestion holds

Textmetadata
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.