MGL2/YMR210w  encodes a monoacylglycerol lipase in  Saccharomyces cerevisiae | Zendy

Selvaraju Kandasamy | Zendy; Gowsalya Ramachandran | Zendy; Vijayakumar Rajendran | Zendy; Nachiappan Vasanthi | Zendy

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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.

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