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J. Biol. Chem., Vol. 277, Issue 38, 35440-35449, September 20, 2002
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From the The YBR159w gene encodes the
major 3-ketoreductase activity of the elongase system of enzymes
required for very long-chain fatty acid (VLCFA) synthesis. Mutants
lacking the YBR159w gene display many of the phenotypes
that have previously been described for mutants with defects in fatty
acid elongation. These phenotypes include reduced VLCFA synthesis,
accumulation of high levels of dihydrosphingosine and phytosphingosine,
and accumulation of medium-chain ceramides. In vitro
elongation assays confirm that the ybr159
The Saccharomyces cerevisiae
YBR159w Gene Encodes the 3-Ketoreductase of the
Microsomal Fatty Acid Elongase*
,,
Department of Biochemistry and Molecular
Biology, Uniformed Services University of the Health Sciences,
Bethesda, Maryland 20184, ¶ Institute of Arable Crops-Long
Ashton Research Station, Long Ashton, Bristol BS41 9AF, United Kingdom,
and the § Department of Molecular Biology, Biochemistry, and
Microbiology, SFB Biomembrane Research Center, University Graz, 1 Schubertstrasse, A8010 Graz, Austria
mutant is
deficient in the reduction of the 3-ketoacyl intermediates of fatty
acid elongation. The ybr159 mutant also displays reduced dehydration of the 3-OH acyl intermediates of fatty acid elongation, suggesting that Ybr159p is required for the stability or function of
the dehydratase activity of the elongase system. Green fluorescent protein-tagged Ybr159p co-localizes and co-immunoprecipitates with
other elongating enzymes, Elo3p and Tsc13p. Whereas VLCFA synthesis is
essential for viability, the ybr159 mutant cells are
viable (albeit very slowly growing) and do synthesize some VLCFA. This
suggested that a functional ortholog of Ybr159p exists that is
responsible for the residual 3-ketoreductase activity. By disrupting
the orthologs of Ybr159w in the ybr159
mutant we found that the ybr159ayr1 double mutant was
inviable, suggesting that Ayr1p is responsible for the residual
3-ketoreductase activity.
*
This work was supported by National Science Foundation Grant
G171FL and Uniformed Services University of the Health Sciences Grant
C071FT (to T. M. D.) and Austrian Science Fund Grant F706 (to
S. D. K.). IACR-Long Ashton Research Station receives grant-aided support from the Biotechnology and Biological Sciences Research Council
of the United Kingdom.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: Dept. of
Biochemistry and Molecular Biology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, MD 20184. Tel.:
301-295-3592; Fax: 301-295-3512; E-mail: tdunn@usuhs.mil.
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