| Structural highlights
Function
HOZ1A_PSESY Serine/threonine-protein acetyltransferase translocated into infected cells, which impairs host microtubule network and host immunity by mediating acetylation of target proteins (PubMed:20636323, PubMed:22319451, PubMed:24204266, PubMed:27525589). Blocks secretion in host cells by mediating acetylation of host tubulin, thereby impairing host microbubule network (PubMed:22319451). Impairs host cell immunity by mediating acetylation of host TIFY/JAZ transcription repressors (Arabidopsis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY9/JAZ10 and TIFY3B/JAZ12), thereby activating host jasmonate signaling (PubMed:24204266, PubMed:27525589).[1] [2] [3] [4]
Publication Abstract from PubMed
Effectors secreted by the type III secretion system are essential for bacterial pathogenesis. Members of the Yersinia outer-protein J (YopJ) family of effectors found in diverse plant and animal pathogens depend on a protease-like catalytic triad to acetylate host proteins and produce virulence. However, the structural basis for this noncanonical acetyltransferase activity remains unknown. Here, we report the crystal structures of the YopJ effector HopZ1a, produced by the phytopathogen Pseudomonas syringae, in complex with the eukaryote-specific cofactor inositol hexakisphosphate (IP6) and/or coenzyme A (CoA). Structural, computational and functional characterizations reveal a catalytic core with a fold resembling that of ubiquitin-like cysteine proteases and an acetyl-CoA-binding pocket formed after IP6-induced structural rearrangements. Modeling-guided mutagenesis further identified key IP6-interacting residues of Salmonella effector AvrA that are required for acetylating its substrate. Our study reveals the structural basis of a novel class of acetyltransferases and the conserved allosteric regulation of YopJ effectors by IP6.
Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family.,Zhang ZM, Ma KW, Yuan S, Luo Y, Jiang S, Hawara E, Pan S, Ma W, Song J Nat Struct Mol Biol. 2016 Aug 15. doi: 10.1038/nsmb.3279. PMID:27525589[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Macho AP, Guevara CM, Tornero P, Ruiz-Albert J, Beuzón CR. The Pseudomonas syringae effector protein HopZ1a suppresses effector-triggered immunity. New Phytol. 2010 Sep;187(4):1018-1033. PMID:20636323 doi:10.1111/j.1469-8137.2010.03381.x
- ↑ Lee AH, Hurley B, Felsensteiner C, Yea C, Ckurshumova W, Bartetzko V, Wang PW, Quach V, Lewis JD, Liu YC, Börnke F, Angers S, Wilde A, Guttman DS, Desveaux D. A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion. PLoS Pathog. 2012 Feb;8(2):e1002523. PMID:22319451 doi:10.1371/journal.ppat.1002523
- ↑ Jiang S, Yao J, Ma KW, Zhou H, Song J, He SY, Ma W. Bacterial effector activates jasmonate signaling by directly targeting JAZ transcriptional repressors. PLoS Pathog. 2013 Oct;9(10):e1003715. PMID:24204266 doi:10.1371/journal.ppat.1003715
- ↑ Zhang ZM, Ma KW, Yuan S, Luo Y, Jiang S, Hawara E, Pan S, Ma W, Song J. Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family. Nat Struct Mol Biol. 2016 Aug 15. doi: 10.1038/nsmb.3279. PMID:27525589 doi:http://dx.doi.org/10.1038/nsmb.3279
- ↑ Zhang ZM, Ma KW, Yuan S, Luo Y, Jiang S, Hawara E, Pan S, Ma W, Song J. Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family. Nat Struct Mol Biol. 2016 Aug 15. doi: 10.1038/nsmb.3279. PMID:27525589 doi:http://dx.doi.org/10.1038/nsmb.3279
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