Critical role of a sheath phosphorylation site on the assembly and\ud function of an atypical type VI secretion system

Autor: Ziveri, J., Chhuon, C., Jamet, A., Rytter, H., Prigent, G., Tros, F., Barel, M., Coureuil, M., Lays, C., Henry, T., Keep, Nicholas H., Guerrera, I.C., Charbit, A.
Jazyk: angličtina
Rok vydání: 2019
Předmět:
ISSN: 1535-9476
Popis: The bacterial pathogen Francisella tularensis possesses a non-canonical type VI secretion\ud system (T6SS) that is required for phagosomal escape in infected macrophages. KCl\ud stimulation has been previously used to trigger assembly and secretion of the T6SS in\ud culture. By differential proteomics, we found here that the amounts of the T6SS proteins\ud remained unchanged upon KCl stimulation, suggesting involvement of post-translational\ud modifications in T6SS assembly. A phosphoproteomic analysis indeed identified a unique\ud phosphorylation site on IglB, a key component of the T6SS sheath. Substitutions of Y139\ud with alanine or phosphomimetics prevented T6SS formation and abolished phagosomal\ud escape whereas substitution with phenylalanine delayed but did not abolish phagosomal\ud escape in J774-1 macrophages. Altogether our data demonstrated that the Y139 site of IglB\ud plays a critical role in T6SS biogenesis, suggesting that sheath phosphorylation could\ud participate to T6SS dynamics.
Databáze: OpenAIRE