This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Finberg, K. E.
Right arrow Articles by Banta, L. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Finberg, K. E.
Right arrow Articles by Banta, L. M.

 Previous Article  |  Next Article 

J. Bacteriol., Sep 1995, 4881-4889, Vol 177, No. 17
Copyright © 1995, American Society for Microbiology

Interactions of VirB9, -10, and -11 with the membrane fraction of Agrobacterium tumefaciens: solubility studies provide evidence for tight associations

KE Finberg, TR Muth, SP Young, JB Maken, SM Heitritter, AN Binns and LM Banta
Department of Biology, Haverford College, Pennsylvania 19041, USA.

The eleven predicted gene products of the Agrobacterium tumefaciens virB operon are believed to form a transmembrane pore complex through which T-DNA export occurs. The VirB10 protein is required for virulence and is a component of an aggregate associated with the membrane fraction of A. tumefaciens. Removal of the putative membrane-spanning domain (amino acids 22 through 55) disrupts the membrane topology of VirB10 (J. E. Ward, E. M. Dale, E. W. Nester, and A. N. Binns, J. Bacteriol. 172:5200-5210, 1990). Deletion of the sequences encoding amino acids 22 to 55 abolishes the ability of plasmid-borne virB10 to complement a null mutation in the virB10 gene, suggesting that the proper topology of VirB10 in the membrane may indeed play a crucial role in T-DNA transfer to the plant cell. Western blot (immunoblot) analysis indicated that the observed loss of virulence could not be attributed to a decrease in the steady-state levels of the mutant VirB10 protein. Although the deletion of the single transmembrane domain would be expected to perturb membrane association, VirB10 delta 22-55 was found exclusively in the membrane fraction. Urea extraction studies suggested that this membrane localization might be the result of a peripheral membrane association; however, the mutant protein was found in both inner and outer membrane fractions separated by sucrose density gradient centrifugation. Both wild-type VirB10 and wild-type VirB9 were only partially removed from the membranes by extraction with 1% Triton X-100, while VirB5 and VirB8 were Triton X-100 soluble.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:

  • den Hartigh, A. B., Rolan, H. G., de Jong, M. F., Tsolis, R. M. (2008). VirB3 to VirB6 and VirB8 to VirB11, but Not VirB7, Are Essential for Mediating Persistence of Brucella in the Reticuloendothelial System. J. Bacteriol. 190: 4427-4436 [Abstract] [Full Text]  
  • Judd, P. K., Mahli, D., Das, A. (2005). Molecular characterization of the Agrobacterium tumefaciens DNA transfer protein VirB6. Microbiology 151: 3483-3492 [Abstract] [Full Text]  
  • Gudlavalleti, S. K., Datta, A. K., Tzeng, Y.-L., Noble, C., Carlson, R. W., Stephens, D. S. (2004). The Neisseria meningitidis Serogroup A Capsular Polysaccharide O-3 and O-4 Acetyltransferase. J. Biol. Chem. 279: 42765-42773 [Abstract] [Full Text]  
  • VanRheenen, S. M., Dumenil, G., Isberg, R. R. (2004). IcmF and DotU Are Required for Optimal Effector Translocation and Trafficking of the Legionella pneumophila Vacuole. Infect. Immun. 72: 5972-5982 [Abstract] [Full Text]  
  • Sexton, J. A., Miller, J. L., Yoneda, A., Kehl-Fie, T. E., Vogel, J. P. (2004). Legionella pneumophila DotU and IcmF Are Required for Stability of the Dot/Icm Complex. Infect. Immun. 72: 5983-5992 [Abstract] [Full Text]  
  • Yeo, H.-J., Waksman, G. (2004). Unveiling Molecular Scaffolds of the Type IV Secretion System. J. Bacteriol. 186: 1919-1926 [Full Text]  
  • Llosa, M., Zunzunegui, S., de la Cruz, F. (2003). Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes. Proc. Natl. Acad. Sci. USA 100: 10465-10470 [Abstract] [Full Text]  
  • Liu, Z., Binns, A. N. (2003). Functional Subsets of the VirB Type IV Transport Complex Proteins Involved in the Capacity of Agrobacterium tumefaciens To Serve as a Recipient in virB-Mediated Conjugal Transfer of Plasmid RSF1010. J. Bacteriol. 185: 3259-3269 [Abstract] [Full Text]  
  • Krall, L., Wiedemann, U., Unsin, G., Weiss, S., Domke, N., Baron, C. (2002). Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacteriumtumefaciens. Proc. Natl. Acad. Sci. USA 99: 11405-11410 [Abstract] [Full Text]  
  • Buttner, D., Nennstiel, D., Klusener, B., Bonas, U. (2002). Functional Analysis of HrpF, a Putative Type III Translocon Protein from Xanthomonas campestris pv. vesicatoria. J. Bacteriol. 184: 2389-2398 [Abstract] [Full Text]  
  • Lee, V. T., Schneewind, O. (2001). Protein secretion and the pathogenesis of bacterial infections. Genes Dev. 15: 1725-1752 [Full Text]  
  • Grahn, A. M., Haase, J., Bamford, D. H., Lanka, E. (2000). Components of the RP4 Conjugative Transfer Apparatus Form an Envelope Structure Bridging Inner and Outer Membranes of Donor Cells: Implications for Related Macromolecule Transport Systems. J. Bacteriol. 182: 1564-1574 [Abstract] [Full Text]  
  • Das, A., Xie, Y.-H. (2000). The Agrobacterium T-DNA Transport Pore Proteins VirB8, VirB9, and VirB10 Interact with One Another. J. Bacteriol. 182: 758-763 [Abstract] [Full Text]  
  • Li, P.-L., Hwang, I., Miyagi, H., True, H., Farrand, S. K. (1999). Essential Components of the Ti Plasmid trb System, a Type IV Macromolecular Transporter. J. Bacteriol. 181: 5033-5041 [Abstract] [Full Text]  
  • Banta, L. M., Bohne, J., Lovejoy, S. D., Dostal, K. (1998). Stability of the Agrobacterium tumefaciens VirB10 Protein Is Modulated by Growth Temperature and Periplasmic Osmoadaption. J. Bacteriol. 180: 6597-6606 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»