Evidence map›Paper›PMID 9023204›Full record

ArticleJournal of bacteriology1997

The lipoprotein VirB7 interacts with VirB9 in the membranes of Agrobacterium tumefaciens.

C Baron, Y R Thorstenson, P C Zambryski

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 97 citations in OpenAlex.

  1. Protein-Protein Interactions: Yeast Two Hybrid.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  2. The VirB System Plays a Crucial Role inInternational journal of molecular sciences · 2021
    Review
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  6. Review
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  9. Review
  10. The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Article
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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

3 authors at 1 institution in 1 country.

C BaronDepartment of Plant and Microbial Biology, University of California at Berkeley, 94720, USA.
Y R Thorstenson
P C Zambryski
University of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

VirB9 and VirB7 are essential components of the putative VirB membrane channel required for transfer of the T-complex from Agrobacterium tumefaciens into plants. In this report, we present a biochemical analysis of their interaction and cellular localization. A comparison of relative electrophoretic mobilities under nonreducing and reducing conditions suggested that they form thiol-sensitive complexes with other proteins. Two-dimensional gel electrophoresis identified one complex as a heterodimer of VirB9 and VirB7 covalently linked by a disulfide bond, as well as VirB7 homodimers and monomers. Immunoprecipitation with VirB9-specific antiserum isolated the heterodimeric VirB9-VirB7 complex. Incubation with reducing agent split the complex into its constituent VirB9 and VirB7, which further confirmed linkage via cysteine residues. The interaction between VirB9 and VirB7 also was observed in the yeast two-hybrid system. Membrane attachment of VirB9-VirB7 may be conferred by lipoprotein modification, since labeling with [3H]palmitic acid in A. tumefaciens verified that VirB7 is a lipoprotein associated with VirB9. VirB9 and VirB7 showed equal distribution between inner and outer membranes, in accord with their proposed association with the transmembrane VirB complex.

Indexed as

Virulence FactorsAgrobacterium tumefaciensBacterial ProteinsCell MembraneCysteineDimerizationElectrophoresis, Polyacrylamide GelLipoproteinsMembrane ProteinsOxidation-ReductionPalmitic AcidPrecipitin TestsBacterial ProteinsCysteineLipoproteinsMembrane ProteinsPalmitic AcidVirulence Factors

Identifiers

PMID9023204
PMCPMC178818
OpenAlexW1882245944

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.