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

Luciana Coutinho Oliveira; Diorge Paulo Souza; Gabriel Umaji Oka; Filipe da Silva Lima; Ronaldo Junio Oliveira; Denize Cristina Favaro; Hans Wienk; Rolf Boelens; Chuck Shaker Farah; Roberto Kopke Salinas

doi:10.1016/j.str.2016.07.015

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

Luciana Coutinho Oliveira, Diorge Paulo Souza^*, Gabriel Umaji Oka, Filipe da Silva Lima, Ronaldo Junio Oliveira, Denize Cristina Favaro, Hans Wienk, Rolf Boelens, Chuck Shaker Farah^*, Roberto Kopke Salinas^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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 β 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.

Original language	English
Pages (from-to)	1707-1718
Number of pages	12
Journal	Structure
Volume	24
Issue number	10
DOIs	https://doi.org/10.1016/j.str.2016.07.015
Publication status	Published - 4 Oct 2016

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10.1016/j.str.2016.07.015

VirB7Final published version, 3.84 MBLicence: Taverne

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

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 β 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.",

author = "Oliveira, {Luciana Coutinho} and Souza, {Diorge Paulo} and Oka, {Gabriel Umaji} and Lima, {Filipe da Silva} and Oliveira, {Ronaldo Junio} and Favaro, {Denize Cristina} and Hans Wienk and Rolf Boelens and Farah, {Chuck Shaker} and Salinas, {Roberto Kopke}",

year = "2016",

month = oct,

day = "4",

doi = "10.1016/j.str.2016.07.015",

language = "English",

volume = "24",

pages = "1707--1718",

journal = "Structure",

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publisher = "Cell Press",

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TY - JOUR

T1 - VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System

AU - Oliveira, Luciana Coutinho

AU - Souza, Diorge Paulo

AU - Oka, Gabriel Umaji

AU - Lima, Filipe da Silva

AU - Oliveira, Ronaldo Junio

AU - Favaro, Denize Cristina

AU - Wienk, Hans

AU - Boelens, Rolf

AU - Farah, Chuck Shaker

AU - Salinas, Roberto Kopke

PY - 2016/10/4

Y1 - 2016/10/4

N2 - 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 β 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.

AB - 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 β 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.

U2 - 10.1016/j.str.2016.07.015

DO - 10.1016/j.str.2016.07.015

M3 - Article

C2 - 27594685

SN - 0969-2126

VL - 24

SP - 1707

EP - 1718

JO - Structure

JF - Structure

IS - 10

ER -

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

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