Evidence map›Paper›PMID 25774531›Full record

ArticlePloS one2015

TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.

Johannes Taubert, Bo Hou, H Jelger Risselada, Denise Mehner, Heinrich Lünsdorf, Helmut Grubmüller, Thomas Brüser

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Secretion of recombinant proteins fromEngineering in life sciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. 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

7 authors at 3 institutions in 1 country.

Johannes TaubertInstitute of Microbiology, Leibniz Universität Hannover, Schneiderberg 50, 30167, Hannover, Germany.
Bo HouInstitute of Microbiology, Leibniz Universität Hannover, Schneiderberg 50, 30167, Hannover, Germany.
H Jelger RisseladaMax Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Denise MehnerInstitute of Microbiology, Leibniz Universität Hannover, Schneiderberg 50, 30167, Hannover, Germany.
Heinrich LünsdorfHelmholtz Centre of Infection Research, Inhoffenstraße 7, 38124, Braunschweig, Germany.
Helmut GrubmüllerMax Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Thomas BrüserInstitute of Microbiology, Leibniz Universität Hannover, Schneiderberg 50, 30167, Hannover, Germany.
Leibniz University Hannover · DEMax Planck Institute for Biophysical Chemistry · DEHelmholtz Centre for Infection Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Tat system can transport folded, signal peptide-containing proteins (Tat substrates) across energized membranes of prokaryotes and plant plastids. A twin-arginine motif in the signal peptide of Tat substrates is recognized by TatC-containing complexes, and TatA permits the membrane passage. Often, as in the model Tat systems of Escherichia coli and plant plastids, a third component - TatB - is involved that resembles TatA but has a higher affinity to TatC. It is not known why most TatA dissociates from TatBC complexes in vivo and distributes more evenly in the membrane. Here we show a TatBC-independent substrate-binding to TatA from Escherichia coli, and we provide evidence that this binding enhances Tat transport. First hints came from in vivo cross-linking data, which could be confirmed by affinity co-purification of TatA with the natural Tat substrates HiPIP and NrfC. Two positions on the surface of HiPIP could be identified that are important for the TatA interaction and transport efficiency, indicating physiological relevance of the interaction. Distributed TatA thus may serve to accompany membrane-interacting Tat substrates to the few TatBC spots in the cells.

Indexed as

Escherichia coliEscherichia coli ProteinsMembrane Transport ProteinsProtein TransportEscherichia coli ProteinsMembrane Transport ProteinsTatA protein, E coliTatB protein, E coliTatC protein, E coli

Identifiers

PMID25774531
PMCPMC4361764
OpenAlexW2070886263

What OpenQuestion holds

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LicenceCC BY
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.