Evidence map›Paper›PMID 22378651›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.

Kush Dalal, Catherine S Chan, Stephen G Sligar, Franck Duong

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.1field-weighted citation impact, top 6% of its field
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

30 citing papers in PubMed, 47 citations in OpenAlex.

  1. Biomolecules · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Profiling theeLife · 2019
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Exploring the existence of lipid rafts in bacteria.Microbiology and molecular biology reviews : MMBR · 2015
    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

4 authors at 2 institutions in 2 countries.

Kush DalalDepartment of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada V6T 1Z3.
Catherine S Chan
Stephen G Sligar
Franck Duong
University of British Columbia · CAUniversity of Illinois Urbana-Champaign · US

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
CIHRNIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM033775
6 · The paper itself

Abstract

The SecA ATPase associates with the SecY complex to push preproteins across the bacterial membrane. Because a single SecY is sufficient to create the conducting channel, the function of SecY oligomerization remains unclear. Here, we have analyzed the translocation reaction using nanodiscs. We show that one SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic lipids supports the activation of the SecA translocation ATPase. In discs, the dimer is predominantly arranged in a back-to-back manner and remains active even if a constituent SecY copy is defective for SecA binding. In membrane vesicles and in intact cells, the coproduction of two inactive SecYs, one for channel gating and the other for SecA binding, recreates a functional translocation unit. These results indisputably argue that the SecY dimer is crucial for the activation of SecA, which is necessary for preprotein transport.

Indexed as

AcidsAdenosine TriphosphatasesBacterial ProteinsEnzyme ActivationGenetic Complementation TestLipidsMembrane Transport ProteinsMutant ProteinsNanostructuresProtein BindingProtein MultimerizationProtein Sorting SignalsProtein TransportSecA ProteinsSEC Translocation ChannelsAcidsAdenosine TriphosphatasesBacterial ProteinsLipidsMembrane Transport ProteinsMutant ProteinsProtein Sorting SignalsSecA ProteinsSEC Translocation Channels

Identifiers

PMID22378651
PMCPMC3306715
OpenAlexW2044775677

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.