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 delta pld1 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, nonplant, phosphatidylcholine-hydrolyzing phospholipase D gene. Because the biological role of PLD is not well understood, we expect that delta pld1 yeast will become a useful tool for the characterization of PLD functions as well as for the identification of mammalian PLD homologs.
Waksman
M
M
Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel. lvjeff@weizmann.ac.il.
Eli
Y
Y
Liscovitch
M
M
Gerst
J E
JE
D000595:Amino Acid Sequence; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010739:Phospholipase D / Q000235:genetics* / Q000378:metabolism; D010944:Plants / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D010739:Phospholipase D