Abstract
Protein prenylation has emerged as an important class of post-translational modifications. The yeast Saccharomyces cerevisiae provides a genetic approach to the analysis of such modifications. Mutants that are defective in farnesylation have been isolated by virtue of their defect in the processing and localization of RAS proteins. This defect confers heat shock resistance on RAS2 Val19 cells, providing a selection for mutant isolation. In this article, we describe the isolation and genetic and biochemical characterization of farnesylation mutants, and discuss their use in the analysis of protein processing.
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