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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Caplan, AJ; Tsai, J; Casey, PJ; Douglas, MG

Published Date

  • September 15, 1992

Published In

Volume / Issue

  • 267 / 26

Start / End Page

  • 18890 - 18895

PubMed ID

  • 1527016

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States