Manda_2018_J.Gen.Appl.Microbiol_64_76

Saccharomyces cerevisiae Ypr147cp was found localized to lipid droplets but the physiological role of Ypr147cp remains unknown. Sequence analysis of Ypr147cp revealed an alpha/beta hydrolase domain along with the conserved GXSXG lipase motif. Recombinant Ypr147cp showed both triacylglycerol lipase and ester hydrolase activities. Knock out of YPR147C led to accumulation of TAG in ypr147cDelta when compared to wild type (WT). In addition, transmission electron microscopic analysis of ypr147cDelta cells revealed a greater number of lipid bodies, justifying the increase in TAG content, and the phenotype was rescued upon overexpression of YPR147C in ypr147cDelta. Moreover, the lipid profiling confirmed the accumulation of fatty acids derived from neutral and phospholipids in ypr147cDelta cells. Based on these results, Ypr147cp is identified as a lipid droplet associated triacylglycerol lipase along with an ester hydrolyzing capacity.