The yeast plasma membrane uracil permease is stabilized against stress induced degradation by a point mutation in a cyclin-like "destruction box"

Biochem Biophys Res Commun. 1994 Jun 15;201(2):769-75. doi: 10.1006/bbrc.1994.1767.


Yeast uracil permease appears to be fairly stable in exponentially growing cells, but it undergoes rapid endocytosis followed by degradation when cells are submitted to adverse conditions, such as nutrient starvation or inhibition of protein synthesis. Uracil permease has a sequence (RIALGSLTD) that is very similar to the "destruction box" of mitotic cyclins. This box is required for the ubiquitin-dependent proteolysis of cyclins. We replaced the invariant arginine residue of the putative "destruction box" in uracil permease by an alanine. The mutation significantly protected the permease against stress-induced degradation. This result suggests that ligation to ubiquitin could be a signal for uracil permease degradation.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / enzymology
  • Consensus Sequence
  • Culture Media
  • Cyclins / genetics*
  • Enzyme Stability
  • Genes, Fungal
  • Kinetics
  • Membrane Transport Proteins / genetics*
  • Membrane Transport Proteins / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nitrogen / metabolism
  • Nucleotide Transport Proteins*
  • Plasmids
  • Point Mutation*
  • Restriction Mapping
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • Species Specificity


  • Culture Media
  • Cyclins
  • FUR4 protein, S cerevisiae
  • Membrane Transport Proteins
  • Nucleotide Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • Nitrogen