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.
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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 |
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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 |
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