D. Taylor, T. Francis, S. Lozinsky, Travis L. Hoffman, M. Giblin, E. Marillia
{"title":"Cloning and characterization of a Constitutive lysophosphatidic acid acyltransferase 2 (LPAT2) gene from Tropaeolum majus L.","authors":"D. Taylor, T. Francis, S. Lozinsky, Travis L. Hoffman, M. Giblin, E. Marillia","doi":"10.2174/1874294701004010007","DOIUrl":null,"url":null,"abstract":"The cloning and characterization of a lyso-phosphatidic acid acyltransferase (LPAT2; EC 2.3.1.51) from Tropaeolum majus from a 20,000 EST collection is described. The 1358 bp TmLPAT2 gene encodes a 42.6 kD polypep- tide; the primary sequence has a membrane bound O-acyltransferase, MBOAT, Box I motif, and Boxes II, III and IV typical of LPATs from various species. Unlike many LPAT2s, the gene was constitutively expressed in all tissues. The TmLPAT2 functionality was confirmed by expression in a yeast LPAT deletion (SLC1 - ) mutant. The TmLPAT2 could use a range of acyl-CoAs as acyl donor, including 22:1-CoA and 20:1-CoA and either 18:1-LPA or 22:1-LPA as acyl acceptor. This new LPAT2 could enable the production of Brassica seed oils with enhanced levels of very long-chain fatty acids.","PeriodicalId":355995,"journal":{"name":"The Open Plant Science Journal","volume":"62 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2010-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"16","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Open Plant Science Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874294701004010007","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 16
Abstract
The cloning and characterization of a lyso-phosphatidic acid acyltransferase (LPAT2; EC 2.3.1.51) from Tropaeolum majus from a 20,000 EST collection is described. The 1358 bp TmLPAT2 gene encodes a 42.6 kD polypep- tide; the primary sequence has a membrane bound O-acyltransferase, MBOAT, Box I motif, and Boxes II, III and IV typical of LPATs from various species. Unlike many LPAT2s, the gene was constitutively expressed in all tissues. The TmLPAT2 functionality was confirmed by expression in a yeast LPAT deletion (SLC1 - ) mutant. The TmLPAT2 could use a range of acyl-CoAs as acyl donor, including 22:1-CoA and 20:1-CoA and either 18:1-LPA or 22:1-LPA as acyl acceptor. This new LPAT2 could enable the production of Brassica seed oils with enhanced levels of very long-chain fatty acids.
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