Evidence map›Paper›PMID 17631633›Full record

ArticleJournal of bacteriology2007

In vivo oligomerization of the F conjugative coupling protein TraD.

Rembrandt J F Haft, Eliora G Gachelet, Tran Nguyen, Luttrell Toussaint, Dylan Chivian, Beth Traxler

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Lipid-Modified Azurin ofFrontiers in microbiology · 2018
    Article
  6. Review
  7. Assembly and mechanisms of bacterial type IV secretion machines.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 1 institution in 1 country.

Rembrandt J F HaftDepartment of Microbiology, University of Washington, Box 357242, Seattle, WA 98195- 7242, USA.
Eliora G Gachelet
Tran Nguyen
Luttrell Toussaint
Dylan Chivian
Beth Traxler
University of Washington · US

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
UW: STIPENDS FOR ASPIRING RESEARCHERST35HL007763 · NHLBI · UNIVERSITY OF WASHINGTON · PI GIBALDI, MILO · 1992 to 2002
$271k
NHLBI NIH HHS T35 HL007763NHLBI NIH HHS T35 HL07763NIGMS NIH HHS T32 GM007270NIGMS NIH HHS T32 GM07270Wellcome Trust
6 · The paper itself

Abstract

Type IV secretory systems are a group of bacterial transporters responsible for the transport of proteins and nucleic acids directly into recipient cells. Such systems play key roles in the virulence of some pathogenic organisms and in conjugation-mediated horizontal gene transfer. Many type IV systems require conserved "coupling proteins," transmembrane polypeptides that are critical for transporting secreted substrates across the cytoplasmic membrane of the bacterium. In vitro evidence suggests that the functional form of coupling proteins is a homohexameric, ring-shaped complex. Using a library of tagged mutants, we investigated the structural and functional organization of the F plasmid conjugative coupling protein TraD by coimmunoprecipitation, cross-linking, and genetic means. We present direct evidence that coupling proteins form stable oligomeric complexes in the membranes of bacteria and that the formation of some of these complexes requires other F-encoded functions. Our data also show that different regions of TraD play distinct roles in the oligomerization process. We postulate a model for in vivo oligomerization and discuss the probable participation of individual domains of TraD in each step.

Indexed as

Conjugation, GeneticCell MembraneCross-Linking ReagentsDimerizationEscherichia coliEscherichia coli ProteinsF FactorMembrane ProteinsModels, MolecularMutationCross-Linking ReagentsEscherichia coli ProteinsMembrane ProteinstraD protein, E coli

Identifiers

PMID17631633
PMCPMC2045173
OpenAlexW2033592488

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.