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J Biol Chem, Vol. 273, Issue 27, 16635-16638, July 3, 1998
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From the The SEC14 gene encodes a
phosphatidylinositol/phosphatidylcholine transfer protein essential for
secretion and growth in yeast (). Mutations (cki1,
cct1, and cpt1) in the CDP-choline pathway for
phosphatidylcholine synthesis suppress the sec14 growth
defect (), permitting sec14ts
cki1, sec14ts cct1, and
sec14ts cpt1 strains to grow at the
sec14ts restrictive temperature. Previously, we
reported that these double mutant strains also excrete the phospholipid
metabolites, choline and inositol (). We now report that these choline
and inositol excretion phenotypes are eliminated when the
SPO14 (PLD1) gene encoding phospholipase D1 is
deleted. In contrast to sec14ts
cki1 strains, sec14ts
cki1 pld1 strains are not viable at the
sec14ts restrictive temperature and exhibit a
pattern of invertase secretion comparable with
sec14ts strains. Thus, the PLD1
gene product appears to play an essential role in the suppression of
the sec14ts defect by CDP-choline pathway
mutations, indicating a role for phospholipase D1 in growth and
secretion. Furthermore, sec14ts strains exhibit
elevated Ca2+-independent, phophatidylinositol
4,5-bisphosphate-stimulated phospholipase D activity. We also propose
that phospholipase D1-mediated phosphatidylcholine turnover generates a
signal that activates transcription of INO1, the structural
gene for inositol 1-phosphate synthase.
Department of Biological Sciences, Carnegie
Mellon University, Pittsburgh, Pennsylvania 15213-2683 and the
§ Institute of Animal Biochemistry and Genetics, Slovak
Academy of Sciences, 90028 Ivanka pri Dunaji, Slovakia
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