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J. Biol. Chem., Vol. 275, Issue 40, 31369-31378, October 6, 2000
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From the In a previous study, we reported that the
Saccharomyces cerevisiae gene YPC1 encodes an
alkaline ceramidase with a dual activity, catalyzing both hydrolysis
and synthesis of yeast ceramide (Mao, C., Xu, R., Bielawska, A., and
Obeid, L. M. (2000) J. Biol. Chem. 275, 6876-6884). In this study, we have identified a YPC1
homologue in S. cerevisiae that also encodes an alkaline
ceramidase. We show that these two ceramidases have different substrate
specificity, such that YPC1p preferentially hydrolyzes phytoceramide,
whereas the new ceramidase YDC1p hydrolyzes dihydroceramide
preferentially and phytoceramide only slightly. Neither enzyme
hydrolyzes unsaturated mammalian-type ceramide. In contrast to YPC1p,
YDC1p had only minor in vitro reverse activity of
catalyzing dihydroceramide formation from a free fatty acid and
dihydrosphingosine and no activity with phytosphingosine.
Overexpression of YDC1p had no reverse activity in non-stressed yeast
cells, but like YPC1p suppressed the inhibition of growth by fumonisin
B1 albeit more modestly. Deletion of YDC1 and
YPC1 or both did not apparently affect growth, suggesting
neither gene is essential. However, the The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF214455.
Cloning and Characterization of a Saccharomyces
cerevisiae Alkaline Ceramidase with Specificity for
Dihydroceramide*
§,§,¶
Division of General Internal Medicine, Ralph
H. Johnson Veterans Affairs Hospital and the ¶ Departments of
Medicine and Biochemistry, Medical University of South Carolina,
Charleston, South Carolina 29425
ydc1 deletion mutant but not the ypc1 deletion mutant was sensitive to
heat stress, indicating a role for dihydroceramide but not
phytoceramide in heat stress responses, and suggesting that the two
enzymes have distinct physiological functions.
*
This work was supported in part by National Institutes of
Health Grants AG16583 and AG12467.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Division of
General Internal Medicine, 114 Doughty St., Rm. 604 STB, P. O. Box 250779, Charleston, SC 29425. Tel.: 843-876-5173; Fax: 843-876-5191; E-mail: obeidl@musc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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