Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae

J Biol Chem. 1992 Sep 15;267(26):18890-5.

Abstract

The Saccharomyces cerevisiae YDJ1 protein (YDJ1p) contains a C-terminal "CaaX box" motif common to proteins that are modified by prenylation. In the present study we show that YDJ1p is a specific substrate for both yeast and mammalian protein farnesyltransferase enzymes in vitro. A mutant form of YDJ1p, in which the conserved cysteine of the CaaX box is mutated to a serine (ydj1-S406p), cannot be farnesylated in vitro. After expression in S. cerevisiae, ydj1-S406p displays a reduced electrophoretic mobility and an increased cytosolic localization in subcellular fractionation experiments when compared to wild type YDJ1p. Expression of ydj1-S406 in cells lacking YDJ1 results in a temperature-sensitive growth phenotype in S. cerevisiae. These data indicate that farnesylation of YDJ1p is required for its function at elevated temperatures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkyl and Aryl Transferases*
  • Electrophoresis, Polyacrylamide Gel
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins*
  • Hot Temperature
  • Mutation
  • Saccharomyces cerevisiae / growth & development*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity
  • Transferases / metabolism

Substances

  • Fungal Proteins
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Saccharomyces cerevisiae Proteins
  • YDJ1 protein, S cerevisiae
  • Transferases
  • Alkyl and Aryl Transferases
  • p21(ras) farnesyl-protein transferase