Structural highlights
Publication Abstract from PubMed
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-RWRKY to position a targeted lysine in the active site for acetylation. Importantly, the PopP2-RRS1-RWRKY association is allosterically regulated by InsP6 binding, suggesting a previously unidentified role of the eukaryote-specific cofactor in substrate interaction. Furthermore, we provide evidence for the reaction intermediate of PopP2-mediated acetylation, an acetyl-cysteine covalent adduct, lending direct support to the 'ping-pong'-like catalytic mechanism proposed for YopJ effectors. Our study provides critical mechanistic insights into the virulence activity of YopJ class of acetyltransferases.
Mechanism of host substrate acetylation by a YopJ family effector.,Zhang ZM, Ma KW, Gao L, Hu Z, Schwizer S, Ma W, Song J Nat Plants. 2017 Jul 24;3:17115. doi: 10.1038/nplants.2017.115. PMID:28737762[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang ZM, Ma KW, Gao L, Hu Z, Schwizer S, Ma W, Song J. Mechanism of host substrate acetylation by a YopJ family effector. Nat Plants. 2017 Jul 24;3:17115. doi: 10.1038/nplants.2017.115. PMID:28737762 doi:http://dx.doi.org/10.1038/nplants.2017.115
