{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["27(3)"],"submitter":["Lauber E"],"funding":["French National Research Agency"],"pubmed_abstract":["Molecular mechanisms underlying quantitative variations of pathogenicity remain elusive. Here, we identified the <i>Xanthomonas campestris</i> XopJ6 effector that triggers disease resistance in cauliflower and <i>Arabidopsis thaliana</i>. XopJ6 is a close homolog of the <i>Ralstonia</i><i>pseudo</i><i>solanacearum</i> PopP2 YopJ family acetyltransferase. XopJ6 is recognized by the RRS1-R/RPS4 NLR pair that integrates a WRKY decoy domain mimicking effector targets. We identified a XopJ6 natural variant carrying a single residue substitution in XopJ6 WRKY-binding site that disrupts interaction with WRKY proteins. This mutation allows XopJ6 to evade immune perception while retaining some XopJ6 virulence functions. Interestingly, <i>xopJ6</i> resides in a Tn<i>3</i>-family transposon likely co"],"journal":["iScience"],"pagination":["109224"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10909901"],"repository":["biostudies-literature"],"pubmed_title":["Bacterial host adaptation through sequence and structural variations of a single type III effector gene."],"pmcid":["PMC10909901"],"pubmed_authors":["Noel LD","Vicedo C","Carrere S","Pichereaux C","Lauber E","Escouboue M","Gris C","Pouzet C","Jauneau A","Deslandes L","Zhang ZM","Gonzalez-Fuente M","Luneau JS"],"additional_accession":[]},"is_claimable":false,"name":"Bacterial host adaptation through sequence and structural variations of a single type III effector gene.","description":"Molecular mechanisms underlying quantitative variations of pathogenicity remain elusive. Here, we identified the <i>Xanthomonas campestris</i> XopJ6 effector that triggers disease resistance in cauliflower and <i>Arabidopsis thaliana</i>. XopJ6 is a close homolog of the <i>Ralstonia</i><i>pseudo</i><i>solanacearum</i> PopP2 YopJ family acetyltransferase. XopJ6 is recognized by the RRS1-R/RPS4 NLR pair that integrates a WRKY decoy domain mimicking effector targets. We identified a XopJ6 natural variant carrying a single residue substitution in XopJ6 WRKY-binding site that disrupts interaction with WRKY proteins. This mutation allows XopJ6 to evade immune perception while retaining some XopJ6 virulence functions. Interestingly, <i>xopJ6</i> resides in a Tn<i>3</i>-family transposon likely co","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-07-15T00:10:23.56Z","creation":"2025-04-19T22:02:56.936Z"},"accession":"S-EPMC10909901","cross_references":{"pubmed":["38439954"],"doi":["10.1016/j.isci.2024.109224"]}}