<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kessler SC</submitter><funding>Australian Research Council</funding><pagination>24243-24250</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7533671</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>117(39)</volume><pubmed_abstract>The necrotrophic fungal pathogen &lt;i>Cochliobolus victoriae&lt;/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 &lt;i>C. victoriae&lt;/i> genome revealed three copies of precursor peptide genes (&lt;i>vicA1-3&lt;/i>) with variable numbers of "GLKLAF" core peptide repeats corresponding to the victorin peptide backbone. &lt;i>vicA1-3&lt;/i> are located in repeat-rich g</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Victorin, the host-selective cyclic peptide toxin from the oat pathogen &lt;i>Cochliobolus victoriae&lt;/i>, is ribosomally encoded.</pubmed_title><pmcid>PMC7533671</pmcid><funding_grant_id>FT160100233</funding_grant_id><funding_grant_id>DP210102180</funding_grant_id><funding_grant_id>DP200101880</funding_grant_id><pubmed_authors>Chooi YH</pubmed_authors><pubmed_authors>Kessler SC</pubmed_authors><pubmed_authors>Zhang X</pubmed_authors><pubmed_authors>Turgeon BG</pubmed_authors><pubmed_authors>McDonald MC</pubmed_authors><pubmed_authors>Rightmyer A</pubmed_authors><pubmed_authors>Lin Z</pubmed_authors><pubmed_authors>Solomon PS</pubmed_authors><pubmed_authors>Gilchrist CLM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Victorin, the host-selective cyclic peptide toxin from the oat pathogen &lt;i>Cochliobolus victoriae&lt;/i>, is ribosomally encoded.</name><description>The necrotrophic fungal pathogen &lt;i>Cochliobolus victoriae&lt;/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 &lt;i>C. victoriae&lt;/i> genome revealed three copies of precursor peptide genes (&lt;i>vicA1-3&lt;/i>) with variable numbers of "GLKLAF" core peptide repeats corresponding to the victorin peptide backbone. &lt;i>vicA1-3&lt;/i> are located in repeat-rich g</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Sep</publication><modification>2026-05-07T15:39:39.289Z</modification><creation>2021-03-16T08:13:05Z</creation></dates><accession>S-EPMC7533671</accession><cross_references><pubmed>32929037</pubmed><doi>10.1073/pnas.2010573117</doi></cross_references></HashMap>