Document Detail

Multiple functions as lipase, steryl ester hydrolase, phospholipase, and acyltransferase of Tgl4p from the yeast Saccharomyces cerevisiae.
MedLine Citation:
PMID:  20332534     Owner:  NLM     Status:  MEDLINE    
Triacylglycerol (TAG) hydrolysis, membrane lipid biosynthesis, and lipid turnover are largely interlinked processes. In yeast, TAG is mobilized by three TAG lipases named Tgl3p, Tgl4p, and Tgl5p, which are localized to lipid particles/droplets. These TAG lipases posses a conserved GXSXG motif that is characteristic of hydrolytic enzymes. Here, we demonstrated that the yeast TAG lipase Tgl4p, the functional ortholog of the adipose TAG lipase, ATGL, catalyzes multiple functions in lipid metabolism. An extended domain and motif search analysis revealed that Tgl4p bears not only a lipase consensus domain but also a conserved motif for calcium-independent phospholipase A(2). We show that Tgl4p exhibits TAG lipase, steryl ester hydrolase, and phospholipase A(2) activities, but surprisingly it also catalyzed the acyl-CoA-dependent acylation of lysophosphatidic acid to phosphatidic acid (PA). Heterologous overexpression of Tgl4p in Pichia pastoris increased total phospholipid and specifically PA synthesis. Moreover, deletion of TGL4 in Saccharomyces cerevisiae showed an altered pattern of phosphatidylcholine and PA molecular species. Altogether, our data suggest that yeast Tgl4p functions as a hydrolytic enzyme in lipid degradation but also contributes to fatty acid channeling and phospholipid remodeling.
Sona Rajakumari; Günther Daum
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-23
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-05-17     Completed Date:  2010-06-14     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15769-76     Citation Subset:  IM    
Institute of Biochemistry, Graz University of Technology, A-8010 Graz, Austria.
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MeSH Terms
Acylation / physiology
Acyltransferases / genetics,  metabolism*
Amino Acid Motifs
Gene Deletion
Lipase / genetics,  metabolism*
Lipid Metabolism / physiology*
Lysophospholipids / genetics,  metabolism
Phosphatidic Acids / genetics,  metabolism
Phosphatidylcholines / genetics,  metabolism
Phospholipases A2 / genetics,  metabolism*
Protein Structure, Tertiary
Saccharomyces cerevisiae / enzymology*,  genetics
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Sterol Esterase / genetics,  metabolism*
Triglycerides / genetics,  metabolism
Grant Support
W 901-B12//Austrian Science Fund FWF
Reg. No./Substance:
0/Lysophospholipids; 0/Phosphatidic Acids; 0/Phosphatidylcholines; 0/Saccharomyces cerevisiae Proteins; 0/Triglycerides; 22002-87-5/lysophosphatidic acid; EC 2.3.-/Acyltransferases; EC Esterase; EC; EC protein, S cerevisiae; EC A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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