Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids

Nils J. Færgeman, C C DiRusso, A Elberger, J Knudsen, P N Black

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The yeast Saccharomyces cerevisiae is able to utilize exogenous fatty acids for a variety of cellular processes including beta-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 microM cerulenin and 500 microM 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.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume272
Issue number13
Pages (from-to)8531-8
Number of pages8
ISSN0021-9258
DOIs
Publication statusPublished - 1997

Keywords

  • 3T3 Cells
  • Adipose Tissue
  • Amino Acid Sequence
  • Animals
  • Boron Compounds
  • Carrier Proteins
  • Cerulenin
  • Fatty Acid Transport Proteins
  • Fatty Acids, Unsaturated
  • Fluorescent Dyes
  • Kinetics
  • Membrane Proteins
  • Membrane Transport Proteins
  • Mice
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Oleic Acid
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

Fingerprint Dive into the research topics of 'Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids'. Together they form a unique fingerprint.

Cite this