{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["98(17)"],"submitter":["Wellesen K"],"pubmed_abstract":["We describe lacerata (lcr) mutants of Arabidopsis, which display various developmental abnormalities, including postgenital organ fusions, and report cloning of the LCR gene by using the maize transposon Enhancer/Suppressor-mutator (En/Spm). The pleiotropic mutant phenotype could be rescued by genetic complementation of lcr mutants with the wild-type LCR gene. The LCR gene encodes a cytochrome P450 monooxygenase, CYP86A8, which catalyzes omega-hydroxylation of fatty acids ranging from C12 to C18:1, as demonstrated by expression of the gene in yeast. Although palmitic and oleic acids were efficient substrates for LCR, 9,10-epoxystearate was not metabolized. Taken together with previous studies, our findings indicate that LCR-dependent omega-hydroxylation of fatty acids could be implicated i"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["9694-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC55514"],"repository":["biostudies-literature"],"pubmed_title":["Functional analysis of the LACERATA gene of Arabidopsis provides evidence for different roles of fatty acid omega -hydroxylation in development."],"pmcid":["PMC55514"],"pubmed_authors":["Pinot F","Nettesheim K","Wisman E","Wellesen K","Durst F","Benveniste I","Yephremov A","Saedler H","Steiner-Lange S"],"additional_accession":[]},"is_claimable":false,"name":"Functional analysis of the LACERATA gene of Arabidopsis provides evidence for different roles of fatty acid omega -hydroxylation in development.","description":"We describe lacerata (lcr) mutants of Arabidopsis, which display various developmental abnormalities, including postgenital organ fusions, and report cloning of the LCR gene by using the maize transposon Enhancer/Suppressor-mutator (En/Spm). The pleiotropic mutant phenotype could be rescued by genetic complementation of lcr mutants with the wild-type LCR gene. The LCR gene encodes a cytochrome P450 monooxygenase, CYP86A8, which catalyzes omega-hydroxylation of fatty acids ranging from C12 to C18:1, as demonstrated by expression of the gene in yeast. Although palmitic and oleic acids were efficient substrates for LCR, 9,10-epoxystearate was not metabolized. Taken together with previous studies, our findings indicate that LCR-dependent omega-hydroxylation of fatty acids could be implicated i","dates":{"release":"2001-01-01T00:00:00Z","publication":"2001 Aug","modification":"2025-04-26T18:11:47.224Z","creation":"2019-03-27T00:12:40Z"},"accession":"S-EPMC55514","cross_references":{"pubmed":["11493698"],"doi":["10.1073/pnas.171285998"]}}