{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ma KW"],"funding":["University of California-Riverside","March of Dimes Foundation","University of California","National Institutes of Health","NIGMS NIH HHS","National Science Foundation"],"pagination":["1157-68"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4768790"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["208(4)"],"pubmed_abstract":["Gram-negative bacteria inject type III secreted effectors (T3SEs) into host cells to manipulate the immune response. The YopJ family effector HopZ1a produced by the plant pathogen Pseudomonas syringae possesses acetyltransferase activity and acetylates plant proteins to facilitate infection. Using mass spectrometry, we identified a threonine residue, T346, as the main autoacetylation site of HopZ1a. Two neighboring serine residues, S349 and S351, are required for the acetyltransferase activity of HopZ1a in vitro and are indispensable for the virulence function of HopZ1a in Arabidopsis thaliana. Using proton nuclear magnetic resonance (NMR), we observed a conformational change of HopZ1a in the presence of inositol hexakisphosphate (IP6), which acts as a eukaryotic co-factor and significantl"],"journal":["The New phytologist"],"pubmed_title":["Two serine residues in Pseudomonas syringae effector HopZ1a are required for acetyltransferase activity and association with the host co-factor."],"pmcid":["PMC4768790"],"funding_grant_id":["IOS-0847870","IOS‐0847870","R01GM092772","R01 GM092772","RO1GM092772","MCB-1054298","MCB‐1054298"],"pubmed_authors":["Ma KW","Coaker G","Pan S","Jiang S","Hawara E","Lee D","Song J","Ma W"],"additional_accession":[]},"is_claimable":false,"name":"Two serine residues in Pseudomonas syringae effector HopZ1a are required for acetyltransferase activity and association with the host co-factor.","description":"Gram-negative bacteria inject type III secreted effectors (T3SEs) into host cells to manipulate the immune response. The YopJ family effector HopZ1a produced by the plant pathogen Pseudomonas syringae possesses acetyltransferase activity and acetylates plant proteins to facilitate infection. Using mass spectrometry, we identified a threonine residue, T346, as the main autoacetylation site of HopZ1a. Two neighboring serine residues, S349 and S351, are required for the acetyltransferase activity of HopZ1a in vitro and are indispensable for the virulence function of HopZ1a in Arabidopsis thaliana. Using proton nuclear magnetic resonance (NMR), we observed a conformational change of HopZ1a in the presence of inositol hexakisphosphate (IP6), which acts as a eukaryotic co-factor and significantl","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Dec","modification":"2025-04-19T01:26:23.839Z","creation":"2019-03-27T02:10:01Z"},"accession":"S-EPMC4768790","cross_references":{"pubmed":["26103463"],"doi":["10.1111/nph.13528"]}}