Evidence map›Paper›PMID 11350936›Full record

ArticleThe EMBO journal2001

Functional reconstitution of bacterial Tat translocation in vitro.

T L Yahr, W T Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. 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
8.3field-weighted citation impact, top 2% 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

56 citing papers in PubMed, 168 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Genome-Wide Identification of Fitness Factors in Seawater forApplied and environmental microbiology · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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
  19. Article
  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

2 authors at 1 institution in 1 country.

T L YahrDepartment of Biochemistry, Dartmouth Medical School, 7200 Vail Building, Hanover, NH 03755-3844, USA.
W T Wickner
Dartmouth College · US

Funding

DYNAMIC SUBUNIT ASSOCIATIONS IN PREPROTEIN TRANSLOCASEF32GM019863 · NIGMS · DARTMOUTH COLLEGE · PI YAHR, TIMOTHY L · 1999 to 2001
$56k
NIGMS NIH HHS F32 GM019863
6 · The paper itself

Abstract

The Tat (twin-arginine translocation) pathway is a Sec-independent mechanism for translocating folded preproteins across or into the inner membrane of Escherichia coli. To study Tat translocation, we sought an in vitro translocation assay using purified inner membrane vesicles and in vitro synthesized substrate protein. While membrane vesicles derived from wild-type cells translocate the Sec-dependent substrate proOmpA, translocation of a Tat-dependent substrate, SufI, was not detected. We established that in vivo overexpression of SufI can saturate the Tat translocase, and that simultaneous overexpression of TatA, B and C relieves this SufI saturation. Using membrane vesicles derived from cells overexpressing TatABC, in vitro translocation of SufI was detected. Like translocation in vivo, translocation of SufI in vitro requires TatABC, an intact membrane potential and the twin-arginine targeting motif within the signal peptide of SUFI: In contrast to Sec translocase, we find that Tat translocase does not require ATP. The development of an in vitro translocation assay is a prerequisite for further biochemical investigations of the mechanism of translocation, substrate recognition and translocase structure.

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsAmino Acid SequenceBiological TransportCarrier ProteinsEscherichia coliGene ExpressionMolecular Sequence DataProtein BiosynthesisCarrier ProteinsEscherichia coli ProteinsMembrane Transport Proteinstwin-arginine translocase complex, E coli

Identifiers

PMID11350936
PMCPMC125449
OpenAlexW2006175108

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.