期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 50, 页码 36061-36072出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.509927
关键词
Lipase; Lipids; Lipid Droplets; Peroxisomes; Triacylglycerol; Yeast
资金
- Austrian Science Fund (FWF) [W901 DK, P23029]
- Austrian Federal Ministry of Science and Research (bmwf)
- Austrian Science Funds, FWF [F3005 SFB LIPOTOX]
- Austrian Science Fund (FWF) [W 901, P 23029] Funding Source: researchfish
- Austrian Science Fund (FWF) [P23029] Funding Source: Austrian Science Fund (FWF)
Background: Triacylglycerols are stored in lipid droplets and can be mobilized by lipases. Results: Ayr1p was identified as a novel triacylglycerol lipase. Conclusion: In addition to the known lipases Tgl3p, Tgl4p, and Tgl5p, further hydrolytic enzymes contribute to the mobilization of non-polar lipids in yeast. Significance: This study opens the view for a broader network of lipolytic enzymes in yeast. Saccharomyces cerevisiae, as well as other eukaryotes, preserves fatty acids and sterols in a biologically inert form, as triacylglycerols and steryl esters. The major triacylglycerol lipases of the yeast S. cerevisiae identified so far are Tgl3p, Tgl4p, and Tgl5p (Athenstaedt, K., and Daum, G. (2003) YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J. Biol. Chem. 278, 23317-23323; Athenstaedt, K., and Daum, G. (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae, are localized to lipid particles. J. Biol. Chem. 280, 37301-37309). We observed that upon cultivation on oleic acid, triacylglycerol mobilization did not come to a halt in a yeast strain deficient in all currently known triacylglycerol lipases, indicating the presence of additional not yet characterized lipases/esterases. Functional proteome analysis using lipase and esterase inhibitors revealed a subset of candidate genes for yet unknown hydrolytic enzymes on peroxisomes and lipid droplets. Based on the conserved GXSXG lipase motif, putative functions, and subcellular localizations, a selected number of candidates were characterized by enzyme assays in vitro, gene expression analysis, non-polar lipid analysis, and in vivo triacylglycerol mobilization assays. These investigations led to the identification of Ayr1p as a novel triacylglycerol lipase of yeast lipid droplets and confirmed the hydrolytic potential of the peroxisomal Lpx1p in vivo. Based on these results, we discuss a possible link between lipid storage, lipid mobilization, and peroxisomal utilization of fatty acids as a carbon source.
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