Document Detail

Redundant systems of phosphatidic acid biosynthesis via acylation of glycerol-3-phosphate or dihydroxyacetone phosphate in the yeast Saccharomyces cerevisiae.
MedLine Citation:
PMID:  10049376     Owner:  NLM     Status:  MEDLINE    
In the yeast Saccharomyces cerevisiae lipid particles harbor two acyltransferases, Gat1p and Slc1p, which catalyze subsequent steps of acylation required for the formation of phosphatidic acid. Both enzymes are also components of the endoplasmic reticulum, but this compartment contains additional acyltransferase(s) involved in the biosynthesis of phosphatidic acid (K. Athenstaedt and G. Daum, J. Bacteriol. 179:7611-7616, 1997). Using the gat1 mutant strain TTA1, we show here that Gat1p present in both subcellular fractions accepts glycerol-3-phosphate and dihydroxyacetone phosphate as a substrate. Similarly, the additional acyltransferase(s) present in the endoplasmic reticulum can acylate both precursors. In contrast, yeast mitochondria harbor an enzyme(s) that significantly prefers dihydroxyacetone phosphate as a substrate for acylation, suggesting that at least one additional independent acyltransferase is present in this organelle. Surprisingly, enzymatic activity of 1-acyldihydroxyacetone phosphate reductase, which is required for the conversion of 1-acyldihydroxyacetone phosphate to 1-acylglycerol-3-phosphate (lysophosphatidic acid), is detectable only in lipid particles and the endoplasmic reticulum and not in mitochondria. In vivo labeling of wild-type cells with [2-3H, U-14C]glycerol revealed that both glycerol-3-phosphate and dihydroxyacetone phosphate can be incorporated as a backbone of glycerolipids. In the gat1 mutant and the 1-acylglycerol-3-phosphate acyltransferase slc1 mutant, the dihydroxyacetone phosphate pathway of phosphatidic acid biosynthesis is slightly preferred as compared to the wild type. Thus, mutations of the major acyltransferases Gat1p and Slc1p lead to an increased contribution of mitochondrial acyltransferase(s) to glycerolipid synthesis due to their substrate preference for dihydroxyacetone phosphate.
K Athenstaedt; S Weys; F Paltauf; G Daum
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  181     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1999 Mar 
Date Detail:
Created Date:  1999-04-07     Completed Date:  1999-04-07     Revised Date:  2012-07-31    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1458-63     Citation Subset:  IM    
Institut für Biochemie und Lebensmittelchemie, Technische Universität, and SFB Biomembrane Research Center, Petersgasse 12/2, A-8010 Graz, Austria.
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MeSH Terms
Acyltransferases / metabolism*
Carbon Radioisotopes
Dihydroxyacetone Phosphate / metabolism*
Endoplasmic Reticulum / enzymology
Fungal Proteins / metabolism
Glycerol / metabolism
Glycerol-3-Phosphate O-Acyltransferase / metabolism
Glycerophosphates / metabolism*
Models, Chemical
Organelles / enzymology
Phosphatidic Acids / biosynthesis*
Phospholipids / metabolism
Radioisotope Dilution Technique
Saccharomyces cerevisiae / enzymology*,  genetics
Saccharomyces cerevisiae Proteins*
Subcellular Fractions / enzymology
Substrate Specificity
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Fungal Proteins; 0/Glycerophosphates; 0/Phosphatidic Acids; 0/Phospholipids; 0/Saccharomyces cerevisiae Proteins; 10028-17-8/Tritium; 56-81-5/Glycerol; 57-03-4/alpha-glycerophosphoric acid; 57-04-5/Dihydroxyacetone Phosphate; EC 2.3.-/Acyltransferases; EC O-Acyltransferase; EC protein, S cerevisiae

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