Dataset Information

Phosphorylation Francisella

ABSTRACT: Francisella possesses a non-canonical T6SS that is essential for efficient phagosomal escape and access to the cytosol of infected macrophages. Using a global and site-specific phosphoproteomic analysis of Francisella we identified here a unique phosphorylation site on IglB, the TssC homologue and a key component of the T6SS contractile sheath. Phosphorylation of the sheath may constitute a previously unrecognized mechanism contributing to the dynamics of assembly-disassembly of the T6SS.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Chiara guerrera

LAB HEAD: Chiara Guerrera

PROVIDER: PXD012507 | Pride | 2023-12-20

REPOSITORIES: Pride

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Publications

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

Ziveri Jason J Chhuon Cerina C Jamet Anne A Rytter Héloïse H Prigent Guénolé G Tros Fabiola F Barel Monique M Coureuil Mathieu M Lays Claire C Henry Thomas T Keep Nicholas H NH Guerrera Ida Chiara IC Charbit Alain A

Molecular & cellular proteomics : MCP 20191002 12

The bacterial pathogen <i>Francisella tularensis</i> 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 i ...[more]

PMID: 31578219

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