Evidence map›Paper›PMID 17568769›Full record

ArticleThe EMBO journal2007

Evidence for a dynamic and transient pathway through the TAT protein transport machinery.

Kenneth Cline, Michael McCaffery

Abstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Review
  3. The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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.

Kenneth ClineHorticultural Sciences Department and Plant Molecular and Cellular Biology, University of Florida, Gainesville FL, USA. kcline@ufl.edu
Michael McCaffery

Funding

TARGETING AND ASSEMBLY OF THYLAKOID MEMBRANE PROTEINSR01GM046951 · NIGMS · UNIVERSITY OF FLORIDA · PI CLINE, KENNETH C. · 1992 to 2011
$2.7M
NIGMS NIH HHS R01 GM046951NIGMS NIH HHS R01 GM46951
6 · The paper itself

Abstract

Tat systems transport completely folded proteins across ion-tight membranes. Three membrane proteins comprise the Tat machinery in most systems. In thylakoids, cpTatC and Hcf106 mediate precursor recognition, whereas Tha4 facilitates translocation. We used chimeric precursor proteins with unstructured peptides and folded domains to test predictions of competing translocation models. Two models invoke protein-conducting channels, whereas another model proposes that cpTatC pulls substrates through a patch of Tha4 on the lipid bilayer. The thylakoid system transported unstructured peptide substrates alone or when fused to folded domains. However, larger substrates stalled before completion, some with amino- and carboxyl-folded domains on opposite sides of the membrane. The length of the precursor that resulted in translocation arrest (20 to 30 nm) exceeded that expected for a single 'pull' mechanism, suggesting that a sustained driving force rather than a single pull moves the protein across the bilayer. Three different methods showed that stalled substrates were not stuck in a channel or even associated with Tat machinery. This finding favors the Tha4 patch model for translocation.

Indexed as

Amino Acid MotifsBacterial ProteinsCell MembraneMembrane Transport ProteinsPeptidesPisum sativumProtein TransportRecombinant ProteinsStaphylococcal Protein AStaphylococcus aureusThylakoidsBacterial ProteinsMembrane Transport ProteinsPeptidesRecombinant ProteinsStaphylococcal Protein A

Identifiers

PMID17568769
PMCPMC1914107

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.