+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

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



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



Journal of Bacteriology 179(3): 583-591



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 delta 1-156, was transdominant in a merodiploid assay, indicating that the C-terminal half of VirB11 contains a protein interaction domain. Products of both virB11 delta 1-156 and virB11 delta 158-343, 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.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 002775780

Download citation: RISBibTeXText

PMID: 9006008


Related references

Characterization of the virB11 ATPase of Agrobacterium tumefaciens Evidence for interaction with other virulence proteins and for at least two domains which contribute to membrane association. Abstracts of the General Meeting of the American Society for Microbiology 96: 542, 1996

Evidence for self-association of the Agrobacterium tumefaciens VirB11 ATPase. Abstracts of the General Meeting of the American Society for Microbiology 98: 341, 1998

Self-assembly of the Agrobacterium tumefaciens VirB11 traffic ATPase. Journal of Bacteriology 182(15): 4137-4145, 2000

Suppression of mutant phenotypes of the Agrobacterium tumefaciens VirB11 ATPase by overproduction of VirB proteins. Journal of Bacteriology 179(18): 5835-5842, 1997

Agrobacterium tumefaciens VirB11 protein requires a consensus nucleotide-binding site for function in virulence. Journal of Bacteriology 177(1): 27-36, 1995

Atpase and autophosphorylation activities determine virulence of virb11 protein in agrobacterium. Abstracts of the General Meeting of the American Society for Microbiology 92: 36, 1992

The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface. Journal of Bacteriology 179(2): 453-462, 1997

The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed to the periplasmic surface. Abstracts of the General Meeting of the American Society for Microbiology 96: 542, 1996

Genetic complementation analysis of the Agrobacterium tumefaciens virB operon: virB2 through virB11 are essential virulence genes. Journal of Bacteriology 176(12): 3646-3660, 1994

Delineation of polar localization domains of Agrobacterium tumefaciens type IV secretion apparatus proteins VirB4 and VirB11. Microbiologyopen 3(5): 793-802, 2014

An inner-membrane-associated virulence protein essential for T-DNA transfer from Agrobacterium tumefaciens to plants exhibits ATPase activity and similarities to conjugative transfer genes. Molecular Microbiology 11(3): 581-588, 1994

Cloning and characterization of the dxs gene, encoding 1-deoxy-d-xylulose 5-phosphate synthase from Agrobacterium tumefaciens, and its overexpression in Agrobacterium tumefaciens. Journal of Biotechnology 128(3): 555-566, 2007

Role of Agrobacterium VirB11 ATPase in T-pilus assembly and substrate selection. Journal of Bacteriology 183(20): 5813-5825, 2001

Partial purification and properties of membrane-bound ATPase in Agrobacterium tumefaciens. Annals of the new York Academy of Sciences 402: 445-449, 1982

The role of membrane atpase in proline and valine transport by agrobacterium tumefaciens. Civerolo, E L , Et Al (Ed ) Current Plant Science And Biotechnology in Agriculture: Plant Pathogenic Bacteria; Sixth International Conference, College Park, Maryland, Usa, June 2-7, 1985 Xxiii+1050p Kluwer Academic Publishers Group: Dordrecht, Netherlands; Boston, Massachusetts, Usa Illus 105, 1987