UCL Discovery
UCL home » Library Services » Electronic resources » UCL Discovery

Critical Role of a Sheath Phosphorylation Site On the Assembly and Function of an Atypical Type VI Secretion System

Ziveri, J; Chhuon, C; Jamet, A; Rytter, H; Prigent, G; Tros, F; Barel, M; ... Charbit, A; + view all (2019) Critical Role of a Sheath Phosphorylation Site On the Assembly and Function of an Atypical Type VI Secretion System. Molecular & Cellular Proteomics , 18 (12) pp. 2418-2432. 10.1074/mcp.RA119.001532. Green open access

[thumbnail of Keep_Critical Role of a Sheath Phosphorylation Site On the Assembly and Function of an Atypical Type VI Secretion System_VoR.pdf]
Preview
Text
Keep_Critical Role of a Sheath Phosphorylation Site On the Assembly and Function of an Atypical Type VI Secretion System_VoR.pdf - Published Version

Download (3MB) | Preview

Abstract

The bacterial pathogen Francisella tularensis possesses a noncanonical type VI secretion system (T6SS) that is required for phagosomal escape in infected macrophages. KCl stimulation has been previously used to trigger assembly and secretion of the T6SS in culture. By differential proteomics, we found here that the amounts of the T6SS proteins remained unchanged upon KCl stimulation, suggesting involvement of post-translational modifications in T6SS assembly. A phosphoproteomic analysis indeed identified a unique phosphorylation site on IglB, a key component of the T6SS sheath. Substitutions of Y139 with alanine or phosphomimetics prevented T6SS formation and abolished phagosomal escape whereas substitution with phenylalanine delayed but did not abolish phagosomal escape in J774-1 macrophages. Altogether our data demonstrated that the Y139 site of IglB plays a critical role in T6SS biogenesis, suggesting that sheath phosphorylation could participate to T6SS dynamics. Data are available via ProteomeXchange with identifier PXD013619; and on MS-Viewer, key lkaqkllxwx.

Type: Article
Title: Critical Role of a Sheath Phosphorylation Site On the Assembly and Function of an Atypical Type VI Secretion System
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1074/mcp.RA119.001532
Publisher version: https://doi.org/10.1074/mcp.RA119.001532
Language: English
Additional information: © 2019 Ziveri et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.This is an Open Access article under theCC BY license (http://creativecommons.org/licenses/by/4.0/).
Keywords: Bacteria, Francisella, IglB, Microbiology, Pathogens, Phosphoproteome, Phosphorylation, Type 6 secretion system
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10119676
Downloads since deposit
17Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item