Mechanism of host substrate acetylation by a YopJ family effector.

ABSTRACT: The Yersinia outer protein J (YopJ) family of bacterial effectors depends on a novel acetyltransferase domain to acetylate signalling proteins from plant and animal hosts. However, the underlying mechanism is unclear. Here, we report the crystal structures of PopP2, a YopJ effector produced by the plant pathogen Ralstonia solanacearum, in complex with inositol hexaphosphate (InsP₆), acetyl-coenzyme A (AcCoA) and/or substrate Resistance to Ralstonia solanacearum 1 (RRS1-R)_WRKY. PopP2 recognizes the WRKYGQK motif of RRS1-R_WRKY to position a targeted lysine in the active site for acetylation. Importantly, the PopP2-RRS1-R_WRKY association is allosterically regulated by InsP₆ binding, suggesting a previously unidentified role of the eukaryo

SUBMITTER: Zhang ZM 

PROVIDER: S-EPMC5546152 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature