{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kessler SC"],"funding":["Australian Research Council"],"pagination":["24243-24250"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7533671"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(39)"],"pubmed_abstract":["The necrotrophic fungal pathogen <i>Cochliobolus victoriae</i> produces victorin, a host-selective toxin (HST) essential for pathogenicity to certain oat cultivars with resistance against crown rust. Victorin is a mixture of highly modified heterodetic cyclic hexapeptides, previously assumed to be synthesized by a nonribosomal peptide synthetase. Herein, we demonstrate that victorin is a member of the ribosomally synthesized and posttranslationally modified peptide (RiPP) family of natural products. Analysis of a newly generated long-read assembly of the <i>C. victoriae</i> genome revealed three copies of precursor peptide genes (<i>vicA1-3</i>) with variable numbers of \"GLKLAF\" core peptide repeats corresponding to the victorin peptide backbone. <i>vicA1-3</i> are located in repeat-rich g"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Victorin, the host-selective cyclic peptide toxin from the oat pathogen <i>Cochliobolus victoriae</i>, is ribosomally encoded."],"pmcid":["PMC7533671"],"funding_grant_id":["FT160100233","DP210102180","DP200101880"],"pubmed_authors":["Chooi YH","Kessler SC","Zhang X","Turgeon BG","McDonald MC","Rightmyer A","Lin Z","Solomon PS","Gilchrist CLM"],"additional_accession":[]},"is_claimable":false,"name":"Victorin, the host-selective cyclic peptide toxin from the oat pathogen <i>Cochliobolus victoriae</i>, is ribosomally encoded.","description":"The necrotrophic fungal pathogen <i>Cochliobolus victoriae</i> produces victorin, a host-selective toxin (HST) essential for pathogenicity to certain oat cultivars with resistance against crown rust. Victorin is a mixture of highly modified heterodetic cyclic hexapeptides, previously assumed to be synthesized by a nonribosomal peptide synthetase. Herein, we demonstrate that victorin is a member of the ribosomally synthesized and posttranslationally modified peptide (RiPP) family of natural products. Analysis of a newly generated long-read assembly of the <i>C. victoriae</i> genome revealed three copies of precursor peptide genes (<i>vicA1-3</i>) with variable numbers of \"GLKLAF\" core peptide repeats corresponding to the victorin peptide backbone. <i>vicA1-3</i> are located in repeat-rich g","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-05-07T15:39:39.289Z","creation":"2021-03-16T08:13:05Z"},"accession":"S-EPMC7533671","cross_references":{"pubmed":["32929037"],"doi":["10.1073/pnas.2010573117"]}}