Four Acyltransferases Uniquely Contribute to Phospholipid Heterogeneity inSaccharomyces cerevisiae
Author(s) -
Peter Oelkers,
Keshav Pokhrel
Publication year - 2016
Publication title -
lipid insights
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.293
H-Index - 14
ISSN - 1178-6353
DOI - 10.4137/lpi.s40597
Subject(s) - acyltransferases , acyltransferase , biochemistry , saccharomyces cerevisiae , phospholipid , glycerophospholipids , phosphatidic acid , yeast , lipidomics , biology , enzyme , chemistry , biosynthesis , membrane
Diverse acyl-CoA species and acyltransferase isoenzymes are components of a complex system that synthesizes glycerophospholipids and triacylglycerols. Saccharomyces cerevisiae has four main acyl-CoA species, two main glycerol-3-phosphate 1- O-acyltransferases (Gat1p, Gat2p), and two main 1-acylglycerol-3-phosphate O-acyltransferases (Lpt1p, Slc1p). The in vivo contribution of these isoenzymes to phospholipid heterogeneity was determined using haploids with compound mutations: gat1Δlpt1Δ, gat2Δlpt1Δ, gat1Δslc1Δ, and gat2Δslc1Δ. All mutations mildly reduced [3H]palmitic acid incorporation into phospholipids relative to triacylglycerol. Electrospray ionization tandem mass spectrometry identified few differences from wild type in gat1Δlpt1Δ, dramatic differences in gat2Δslc1Δ, and intermediate changes in gat2Δlpt1Δ and gat1Δslc1Δ. Yeast expressing Gat1p and Lpt1p had phospholipids enriched with acyl chains that were unsaturated, 18 carbons long, and paired for length. These alterations prevented growth at 18.5°C and in 10% ethanol. Therefore, Gat2p and Slc1p dictate phospholipid acyl chain composition in rich media at 30°C. Slc1p selectively pairs acyl chains of different lengths.
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