TagR promotes PpkA-catalysed type VI secretion activation in Pseudomonas aeruginosa.

ABSTRACT: Type VI secretion systems (T6SSs) contribute to interactions of bacterial pathogens and symbionts with their hosts. Previously, we showed that Pseudomonas aeruginosa T6S is posttranslationally activated upon phosphorylation of Fha1, an FHA domain protein, by PpkA, a membrane-spanning threonine kinase. Herein, additional structural, enzymatic and genetic requirements for PpkA-catalysed T6SS activation are identified. We found that PpkA plays an essential structural role in the T6SS, and that this role is intimately linked to its ability to promote secretion and phosphorylate Fha1. Protein localization and protein-protein interaction studies show that a complex containing Fha1 and the T6S ATPase, ClpV1 is recruited to the T6S apparatus in a phosphorylation-dependent manner. The mechanism of

SUBMITTER: Hsu F 

PROVIDER: S-EPMC3402362 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature