title: Modification of seed oil content and acyl composition in the brassicaceae by expression of a yeast sn-2 acyltransferase gene.
abstract: A putative yeast sn-2 acyltransferase gene (SLC1-1), reportedly a variant acyltransferase that suppresses a genetic defect in sphingolipid long-chain base biosynthesis, has been expressed in a yeast SLC deletion strain. The SLC1-1 gene product was shown in vitro to encode an sn-2 acyltransferase capable of acylating sn-1 oleoyl-lysophosphatidic acid, using a range of acyl-CoA thioesters, including 18:1-, 22:1-, and 24:0-CoAs. The SLC1-1 gene was introduced into Arabidopsis and a high erucic acid-containing Brassica napus cv Hero under the control of a constitutive (tandem cauliflower mosaic virus 35S) promoter. The resulting transgenic plants showed substantial increases of 8 to 48% in seed oil content (expressed on the basis of seed dry weight) and increases in both overall proportions and amounts of very-long-chain fatty acids in seed triacylglycerols (TAGs). Furthermore, the proportion of very-long-chain fatty acids found at the sn-2 position of TAGs was increased, and homogenates prepared from developing seeds of transformed plants exhibited elevated lysophosphatidic acid acyltransferase (EC 2.3.1.51) activity. Thus, the yeast sn-2 acyltransferase has been shown to encode a protein that can exhibit lysophosphatidic acid acyltransferase activity and that can be used to change total fatty acid content and composition as well as to alter the stereospecific acyl distribution of fatty acids in seed TAGs.
authors.affiliation: National Research Council of Canada, Plant Biotechnology Institute, Saskatoon, Saskatchewan, Canada.
authors.forename: J
authors.initials: J
authors.lastname: Zou
authors.forename: V
authors.initials: V
authors.lastname: Katavic
authors.forename: E M
authors.initials: EM
authors.lastname: Giblin
authors.forename: D L
authors.initials: DL
authors.lastname: Barton
authors.forename: S L
authors.initials: SL
authors.lastname: MacKenzie
authors.forename: W A
authors.initials: WA
authors.lastname: Keller
authors.forename: X
authors.initials: X
authors.lastname: Hu
authors.forename: D C
authors.initials: DC
authors.lastname: Taylor
mesh_terms: D051103:1-Acylglycerol-3-Phosphate O-Acyltransferase; D000215:Acylation; D000217:Acyltransferases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D000483:Alleles; D017360:Arabidopsis; D001937:Brassica / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D004398:Dyneins; D005227:Fatty Acids / Q000032:analysis; D005656:Fungal Proteins / Q000096:biosynthesis / Q000235:genetics*; D017343:Genes, Plant; D016153:Genes, Suppressor; D010938:Plant Oils / Q000032:analysis*; D030821:Plants, Genetically Modified / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D012639:Seeds / Q000737:chemistry*; D014280:Triglycerides / Q000032:analysis
chemical_list: D005227:Fatty Acids; D005656:Fungal Proteins; D010938:Plant Oils; D029701:Saccharomyces cerevisiae Proteins; D014280:Triglycerides; D000217:Acyltransferases; D051103:1-Acylglycerol-3-Phosphate O-Acyltransferase; D004398:Dyneins; C083745:SLC1 protein, S cerevisiae