Evidence map›Paper›PMID 9006008›Full record

ArticleJournal of bacteriology1997

Characterization of membrane and protein interaction determinants of the Agrobacterium tumefaciens VirB11 ATPase.

S Rashkova, G M Spudich, P J Christie

Open access · greenAbstract 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 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 84 citations in OpenAlex.

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  11. Review
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  14. Biological diversity of prokaryotic type IV secretion systems.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  15. The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009
    Review
  16. Article
  17. 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.

S RashkovaDepartment of Microbiology and Molecular Genetics, The University of Texas Health Science Center at Houston, 77030, USA.
G M Spudich
P 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
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 R01 GM048746
6 · The paper itself

Abstract

The VirB11 ATPase is a putative component of the transport machinery responsible for directing the export of nucleoprotein particles (T complexes) across the Agrobacterium tumefaciens envelope to susceptible plant cells. Fractionation and membrane treatment studies showed that approximately 30% of VirB11 partitioned as soluble protein, whereas the remaining protein was only partially solubilized with urea from cytoplasmic membranes of wild-type strain A348 as well as a Ti-plasmidless strain expressing virB11 from an IncP replicon. Mutations in virB11 affecting protein function were mapped near the amino terminus (Q6L, P13L, and E25G), just upstream of a region encoding a Walker A nucleotide-binding site (F154H;L155M), and within the Walker A motif (P170L, K175Q, and delta GKT174-176). The K175Q and delta GKT174-176 mutant proteins partitioned almost exclusively with the cytoplasmic membrane, suggesting that an activity associated with nucleotide binding could modulate the affinity of VirB11 for the cytoplasmic membrane. The virB11F154H;L155M allele was transdominant over wild-type virB11 in a merodiploid assay, providing strong evidence that at least one form of VirB11 functions as a homo- or heteromultimer. An allele with a deletion of the first half of the gene, virB11 delta1-156, was transdominant in a merodiploid assay, indicating that the C-terminal half of VirB11 contains a protein interaction domain. Products of both virB11 delta1-156 and virB11 delta158-343, which synthesizes the N-terminal half of VirB11, associated tightly with the A. tumefaciens membrane, suggesting that both halves of VirB11 contain membrane interaction determinants.

Indexed as

Virulence FactorsAdenosine TriphosphatasesAgrobacterium tumefaciensBacterial ProteinsBinding SitesCell CompartmentationCell MembraneDNA Mutational AnalysisMutationPhenotypePlantsProtein BindingSequence DeletionStructure-Activity RelationshipAdenosine TriphosphatasesBacterial ProteinsVirulence Factors

Identifiers

PMID9006008
PMCPMC178735
OpenAlexW2041548140

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.