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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System

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Author(s):
Oliveira, Luciana Coutinho ; Souza, Diorge Paulo ; Oka, Gabriel Umaji ; Lima, Filipe da Silva ; Oliveira, Ronaldo Junio ; Favaro, Denize Cristina ; Wienk, Hans ; Boelens, Rolf ; Farah, Chuck Shaker ; Salinas, Roberto Kopke
Total Authors: 10
Document type: Journal article
Source: Structure; v. 24, n. 10, p. 1707-1718, OCT 4 2016.
Web of Science Citations: 3
Abstract

The type IV secretion system (T4SS) from the phytopathogen Xanthomonas citri (Xac) is a bactericidal nanomachine. The T4SS core complex is a ring composed of multiple copies of VirB7-VirB9-VirB10 subunits. Xac-VirB7 contains a disordered N-terminal tail (VirB7(NT)) that recognizes VirB9, and a C-terminal domain (VirB7(CT)) involved in VirB7 self-association. Here, we show that VirB7(NT) forms a short beta strand upon binding to VirB9 and stabilizes it. A tight interaction between them is essential for T4SS assembly and antibacterial activity. Abolishing VirB7 self-association or deletion of the VirB7 C-terminal domain impairs this antibacterial activity without disturbing T4SS assembly. These findings reveal protein interactions within the core complex that are critical for the stability and activity of a T4SS. (AU)

FAPESP's process: 13/17883-2 - Structure and dynamics of the Na+/Ca2+ exchanger from Drosophila melanogaster
Grantee:Roberto Kopke Salinas
Support type: Regular Research Grants
FAPESP's process: 11/07777-5 - Cyclic di-GMP signaling and the Type IV macromolecule secretion system in Xanthomonas citri
Grantee:Shaker Chuck Farah
Support type: Research Projects - Thematic Grants