Agrobacterium type IV secretion is a two‐step process in which export substrates associate with the virulence protein VirJ in the periplasm

Agrobacterium type IV secretion is a two‐step process in which export substrates associate with... Summary Type IV secretion systems are virulence determinants in many bacteria and share extensive homology with many conjugal transfer systems. Although type IV systems and their homologues have been studied widely, the mechanism by which substrates are secreted remains unclear. In Agrobacterium, we show that type IV secretion substrates that lack signal peptides form a soluble complex in the periplasm with the virulence protein VirJ. Additionally, these proteins co‐precipitate with constituents of the type IV transporter: the VirB pilus and the VirD4 protein. Our findings suggest that the substrate proteins localized to the periplasm may associate with the pilus in a manner that is mediated by VirJ, and suggest a two‐step process for type IV secretion in Agrobacterium. Our analyses of protein–protein interactions in a variety of mutant backgrounds indicate that substrates are probably secreted independently of one another. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Microbiology Wiley

Agrobacterium type IV secretion is a two‐step process in which export substrates associate with the virulence protein VirJ in the periplasm

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Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0950-382X
eISSN
1365-2958
DOI
10.1046/j.1365-2958.2002.03098.x
Publisher site
See Article on Publisher Site

Abstract

Summary Type IV secretion systems are virulence determinants in many bacteria and share extensive homology with many conjugal transfer systems. Although type IV systems and their homologues have been studied widely, the mechanism by which substrates are secreted remains unclear. In Agrobacterium, we show that type IV secretion substrates that lack signal peptides form a soluble complex in the periplasm with the virulence protein VirJ. Additionally, these proteins co‐precipitate with constituents of the type IV transporter: the VirB pilus and the VirD4 protein. Our findings suggest that the substrate proteins localized to the periplasm may associate with the pilus in a manner that is mediated by VirJ, and suggest a two‐step process for type IV secretion in Agrobacterium. Our analyses of protein–protein interactions in a variety of mutant backgrounds indicate that substrates are probably secreted independently of one another.

Journal

Molecular MicrobiologyWiley

Published: Sep 1, 2002

References

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