Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae.
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.
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Related Subject Headings
- Transferases
- Substrate Specificity
- Saccharomyces cerevisiae Proteins
- Saccharomyces cerevisiae
- Mutation
- Hot Temperature
- Heat-Shock Proteins
- HSP40 Heat-Shock Proteins
- Fungal Proteins
- Electrophoresis, Polyacrylamide Gel
Citation
Published In
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Transferases
- Substrate Specificity
- Saccharomyces cerevisiae Proteins
- Saccharomyces cerevisiae
- Mutation
- Hot Temperature
- Heat-Shock Proteins
- HSP40 Heat-Shock Proteins
- Fungal Proteins
- Electrophoresis, Polyacrylamide Gel