Evidence map›Paper›PMID 19656854›Full record

ArticleMolecular biology of the cell2009

Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.

Fu-Cheng Liang, Umesh K Bageshwar, Siegfried M Musser

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Direct visualization of theScience advances · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. 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
  15. Direct simulation of early-stage Sec-facilitated protein translocation.Journal of the American Chemical Society · 2012
    Article
  16. Article
  17. SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011
    Review
  18. Article
  19. 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 at 1 institution in 1 country.

Fu-Cheng LiangDepartment of Molecular and Cellular Medicine, College of Medicine, The Texas A&M Health Science Center, College Station, TX 77843, USA.
Umesh K Bageshwar
Siegfried M Musser
Texas A&M Health Science Center · US

Funding

Single Molecule Analysis of Bacterial Protein TransportR01GM065534 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI MUSSER, SIEGFRIED M · 2003 to 2010
$1.6M
NIGMS NIH HHS GM065534NIGMS NIH HHS R01 GM065534
6 · The paper itself

Abstract

An in vitro real-time single turnover assay for the Escherichia coli Sec transport system was developed based on fluorescence dequenching. This assay corrects for the fluorescence quenching that occurs when fluorescent precursor proteins are transported into the lumen of inverted membrane vesicles. We found that 1) the kinetics were well fit by a single exponential, even when the ATP concentration was rate-limiting; 2) ATP hydrolysis occurred during most of the observable reaction period; and 3) longer precursor proteins transported more slowly than shorter precursor proteins. If protein transport through the SecYEG pore is the rate-limiting step of transport, which seems likely, these conclusions argue against a model in which precursor movement through the SecYEG translocon is mechanically driven by a series of rate-limiting, discrete translocation steps that result from conformational cycling of the SecA ATPase. Instead, we propose that precursor movement results predominantly from Brownian motion and that the SecA ATPase regulates pore accessibility.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAdenylyl ImidodiphosphateBacterial Outer Membrane ProteinsBacterial ProteinsDose-Response Relationship, DrugEscherichia coliEscherichia coli ProteinsKineticsMembrane Transport ProteinsMutationNickelProtein PrecursorsProtein TransportSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesAdenosine TriphosphateAdenylyl ImidodiphosphateBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsNickelouter membrane protein A precursor (E coli)Protein PrecursorsSecA ProteinsSEC Translocation ChannelsSuccinic Acid

Identifiers

PMID19656854
PMCPMC2754939
OpenAlexW2065199261

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.