Identification and Characterization of a Gene Encoding Phospholipase D Activity in Yeast

We have identified an open reading frame on chromosome XI of the yeast, Saccharomyces cerevisiae, as encoding a protein with phospholipase D (PLD) activity. We have named this open reading frame, PLD1, and show that yeast bearing a disruption in this gene are unable to catalyze the hydrolysis of phosphatidylcholine. PLD1 encodes a hypothetical protein of 1683 amino acids and has a predicted molecular mass of 195 kDa. Yeast bearing disruptions at the PLD1 locus are morphologically normal and grow vegetatively like wild-type cells. In contrast, homozygous Δpld1 diploid cells are unable to sporulate and do not produce asci under conditions that induce meiosis and sporulation in wild-type cells. Thus, PLD1 is likely to be essential for the meiotic cycle in yeast cells.This is the first identification of a eukaryotic, non-plant, phosphatidylcholine-hydrolyzing phospholipase D gene. Because the biological role of PLD is not well understood, we expect that Δpld1 yeast will become a useful tool for the characterization of PLD functions as well as for the identification of mammalian PLD homologs. We have identified an open reading frame on chromosome XI of the yeast, Saccharomyces cerevisiae, as encoding a protein with phospholipase D (PLD) activity. We have named this open reading frame, PLD1, and show that yeast bearing a disruption in this gene are unable to catalyze the hydrolysis of phosphatidylcholine. PLD1 encodes a hypothetical protein of 1683 amino acids and has a predicted molecular mass of 195 kDa. Yeast bearing disruptions at the PLD1 locus are morphologically normal and grow vegetatively like wild-type cells. In contrast, homozygous Δpld1 diploid cells are unable to sporulate and do not produce asci under conditions that induce meiosis and sporulation in wild-type cells. Thus, PLD1 is likely to be essential for the meiotic cycle in yeast cells. This is the first identification of a eukaryotic, non-plant, phosphatidylcholine-hydrolyzing phospholipase D gene. Because the biological role of PLD is not well understood, we expect that Δpld1 yeast will become a useful tool for the characterization of PLD functions as well as for the identification of mammalian PLD homologs.