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FSH1 encodes lysophospholipase activity in Saccharomyces cerevisiae.

Biotechnol Lett. 2021 Jan;43(1):279-286. Epub 2020 Sep 12
Gowsalya Ramachandran 1 , Ravi Chidambaram 1 , Vasanthi Nachiappan 2
Gowsalya Ramachandran 1 , Ravi Chidambaram 1 , Vasanthi Nachiappan 2

[No authors listed]

Author information
  • 1 Department of Biochemistry, School of Life Sciences, Bharathidasan University, Tiruchirappalli, 620024, Tamil Nadu, India.
  • 2 Department of Biochemistry, School of Life Sciences, Bharathidasan University, Tiruchirappalli, 620024, Tamil Nadu, India. vasanthibch@gmail.com.

摘要


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).

KEYWORDS: FFA, FSH1, Lipid droplets, Phospholipase, Phospholipids