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Geranylgeranyltransferase I (GGTase I) catalyzes the transfer of a prenyl group from geranylgeranyl diphosphate to the carboxy-terminal cysteine of proteins with a motif referred to as a CaaX box (C, cysteine; a, usually aliphatic amino acid; X, usually L). The α and β subunits of GGTase I fromSaccharomyces cerevisiae are encoded byRAM2 andCDC43 , respectively, and each is essential for viability. We are evaluating GGTase I as a potential target for antimycotic therapy of the related yeast,Candida albicans , which is the major human pathogen for disseminated fungal infections. Recently we clonedCaCDC43 , theC. albicans homolog ofS. cerevisiae CDC43 . To study its role inC. albicans , both alleles were sequentially disrupted in strain CAI4. NullCacdc43 mutants were viable despite the lack of detectable GGTase I activity but were morphologically abnormal. The subcellular distribution of two GGTase I substrates, Rho1p and Cdc42p, was shifted from the membranous fraction to the cytosolic fraction in thecdc43 mutants, and levels of these two proteins were elevated compared to those in the parent strain. Two compounds that are potent GGTase I inhibitors in vitro but that have poor antifungal activity, J-109,390 and L-269,289, caused similar changes in the distribution and quantity of the substrate. The lethality of anS. cerevisiae cdc43 mutant can be suppressed by simultaneous overexpression ofRHO1 andCDC42 on high-copy-number plasmids (Y. Ohya et al., Mol. Biol. Cell 4:1017, 1991; C. A. Trueblood, Y. Ohya, and J. Rine, Mol. Cell. Biol. 13:4260, 1993). Prenylation presumably occurs by farnesyltransferase (FTase). We hypothesize that Cdc42p and Rho1p ofC. albicans can be prenylated by FTase when GGTase I is absent or limiting and that elevation of these two substrates enables them to compete with FTase substrates for prenylation and thus allows sustained growth.

Geranylgeranyltransferase I of Candida albicans : Null Mutants or Enzyme Inhibitors Produce Unexpected Phenotypes