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MGL2/YMR210w encodes a monoacylglycerol lipase in Saccharomyces cerevisiae
Author(s) -
Selvaraju Kandasamy,
Gowsalya Ramachandran,
Vijayakumar Rajendran,
Nachiappan Vasanthi
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12136
Subject(s) - monoacylglycerol lipase , lipase , saccharomyces cerevisiae , open reading frame , biochemistry , mutant , chemistry , phenotype , enzyme , microbiology and biotechnology , biology , gene , peptide sequence , endocannabinoid system , receptor
In silico analysis of the uncharacterized open reading frame YMR210w in Saccharomyces cerevisiae revealed that it possesses both an α/β hydrolase domain (ABHD) and a typical lipase ( GXSXG) motif. The purified protein displayed monoacylglycerol (MAG) lipase activity and preferred palmitoyl‐MAG. Overexpression of YMR210w in the known MAG lipase mutant yju3 Δ clearly revealed that the protein had MAG lipase activity, hence we named the ORF MGL2 . Overexpression of YMR210w decreased the cellular triacylglycerol levels. Analysis of the overexpressed strains showed reduction in the lipid droplets number and size. Phenotype studies revealed that the double deletion yju3 Δ mgl2 Δ displayed a growth defect that was partially restored by MGL2 overexpression.