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(Received for publication, December 2, 1996, and in revised form, January 2, 1997)
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From the ¶ Department of Biochemistry and Molecular Biology,
The Albany Medical College, Albany, New York 12208, the
The yeast Saccharomyces cerevisiae is
able to utilize exogenous fatty acids for a variety of cellular
processes including 
Department of Biochemistry, University of Tennessee
College of Medicine, Memphis, Tennessee 38163, the
§ Institute of Biochemistry, Odense University, DK-5230
Odense, Denmark, and the 
Department of Anatomy and Neurobiology,
University of Tennessee College of Medicine,
Memphis, Tennessee 38163
-oxidation, phospholipid biosynthesis, and
protein modification. The molecular mechanisms that govern the uptake
of these compounds in S. cerevisiae have not been
described. We report the characterization of FAT1, a gene
that encodes a putative membrane-bound long-chain fatty acid transport
protein (Fat1p). Fat1p contains 623 amino acid residues that are 33%
identical and 54% with similar chemical properties as compared with
the fatty acid transport protein FATP described in 3T3-L1 adipocytes
(Schaffer and Lodish (1994) Cell 79, 427-436), suggesting
a similar function. Disruption of FAT1 results in 1) an
impaired growth in YPD medium containing 25 µM cerulenin
and 500 µM fatty acid (myristate (C14:0),
palmitate (C16:0), or oleate (C18:1)); 2) a
marked decrease in the uptake of the fluorescent long-chain fatty acid
analogue boron dipyrromethene difluoride dodecanoic acid (BODIPY-3823);
3) a reduced rate of exogenous oleate incorporation into phospholipids;
and 4) a 2-3-fold decrease in the rates of oleate uptake. These data
support the hypothesis that Fat1p is involved in long-chain fatty acid
uptake and may represent a long-chain fatty acid transport protein.
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