Evidence map›Paper›PMID 12270814›Full record

ArticleJournal of bacteriology2002

A novel cytology-based, two-hybrid screen for bacteria applied to protein-protein interaction studies of a type IV secretion system.

Zhiyong Ding, Zhenming Zhao, Simon J Jakubowski, Atmakuri Krishnamohan, William Margolin, Peter J Christie

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 55 citations in OpenAlex.

  1. A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. ParP prevents dissociation of CheA from chemotactic signaling arrays and tethers them to a polar anchor.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

6 authors at 1 institution in 1 country.

Zhiyong DingDepartment of Microbiology and Molecular Genetics, The University of Texas--Houston Medical School, Houston, Texas 77030, USA.
Zhenming Zhao
Simon J Jakubowski
Atmakuri Krishnamohan
William Margolin
Peter J Christie
The University of Texas Health Science Center at Houston · US

Funding

TRANSLOCATION OF DNA ACROSS THE AGROBACTERIUM ENVELOPER01GM048746 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CHRISTIE, PETER J. · 1998 to 2018
$6.9M
Targeting and assembly of E. coli division proteinsR01GM061074 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MARGOLIN, WILLIAM · 2000 to 2018
$5.7M
TRANSLOCATION OF DNA ACROSS THE AGROBACTERIUM ENVELOPER29GM048746 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CHRISTIE, PETER J. · 1993 to 1997
–
NIGMS NIH HHS GM48746NIGMS NIH HHS GM61074NIGMS NIH HHS R01 GM048746NIGMS NIH HHS R01 GM061074
6 · The paper itself

Abstract

DivIVA of Bacillus subtilis and FtsZ of Escherichia coli were used to target heterologous protein complexes to cell division sites of E. coli and Agrobacterium tumefaciens. DivIVA and FtsZ that were fused to the dimerizing leucine zipper (LZ) domain of the yeast transcription activator GCN4 directed the green fluorescent protein (GFP) that was fused to an LZ domain to E. coli division sites, resulting in fluorescence patterns identical to those observed with DivIVA::GFP and FtsZ::GFP. These cell division proteins also targeted the VirE1 chaperone and VirE2 secretion substrate complex to division sites of E. coli and A. tumefaciens. Coproduction of the native VirE1 or VirE2 proteins inhibited the dihybrid interaction in both species, as judged by loss of GFP targeting to division sites. The VirE1 chaperone bound independently to N- and C-terminal regions of VirE2, with a requirement for residues 84 to 147 and 331 to 405 for these interactions, as shown by dihybrid studies with VirE1::GFP and DivIVA fused to N- and C-terminal VirE2 fragments. DivIVA also targeted homo- and heterotypic complexes of VirB8 and VirB10, two bitopic inner membrane subunits of the A. tumefaciens T-DNA transfer system, in E. coli and homotypic complexes of VirB10 in A. tumefaciens. VirB10 self-association in bacteria was mediated by the C-terminal periplasmic domain, as shown by dihybrid studies with fusions to VirB10 truncation derivatives. Together, our findings establish a proof-of-concept for the use of cell-location-specific proteins for studies of interactions among cytosolic and membrane proteins in diverse bacterial species.

Indexed as

Cytoskeletal ProteinsDNA-Binding ProteinsTwo-Hybrid System TechniquesAgrobacterium tumefaciensBacillus subtilisBacterial ProteinsCell Cycle ProteinsCell DivisionDNA, BacterialEscherichia coliLeucine ZippersMembrane ProteinsProtein BindingProtein KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsDivIVA protein, bacteriaDNA, BacterialDNA-Binding ProteinsFtsZ protein, BacteriaMembrane ProteinsProtein KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsT-DNA

Identifiers

PMID12270814
PMCPMC139600
OpenAlexW2107842163

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.