FSH1 encodes lysophospholipase activity in Saccharomyces cerevisiae.

Biotechnol Lett

Department of Biochemistry, School of Life Sciences, Bharathidasan University, Tiruchirappalli, 620024, Tamil Nadu, India.

Published: January 2021

Objectives: To elucidate the role of FSH1 (family of serine hydrolase) in lipid homeostasis.

Results: Proteins in various species containing alpha/beta hydrolase domain are known to be involved in lipid metabolism. In silico analysis of the FSH1 gene in Saccharomyces cerevisiae revealed the presence of alpha/beta hydrolase domain (ABHD) and a lipase motif (GXSXG), however its function in lipid metabolism remained elusive. The overexpression of FSH1 in WT and fsh1Δ cells showed a significant reduction in the cellular phospholipid levels and an increase in the triacylglycerol levels and lipid droplet (LD) number. Furthermore, the purified recombinant protein Fsh1p was identified as a lysophospholipase that specifically acts on lysophosphatidylserine (LPS) and impacts the lipid homeostasis in S. cerevisiae.

Conclusions: These results depicted that Fsh1p has a role on lipid homeostasis and is a lysophospholipase that hydrolyzes lysophosphatidylserine (LPS).

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http://dx.doi.org/10.1007/s10529-020-03004-xDOI Listing

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