Occurrence and biochemical characterization of GTP-binding proteins in Candida albicans

The activities of GTP-binding and GTPase in Candida albicans were present in the cytosol, KCl- and cholate-extractable fractions. At least two kinds of GTP-binding proteins were found in the cytosolic fraction; the major one with a molecular mass of about 30 kDa and the other about 500 kDa. The former specifically bound guanine nucleotides and was most likely to bind GDP since guanosine 5'-O-(thio) triphosphate (GTP gamma S)-binding was accelerated by addition of (NH4)2SO4. The latter showed no specificity in nucleotide binding and could also bind adenine nucleotides. The proteins were not ADP-ribosylated by either pertussis toxin or cholera toxin. These results indicate that ras-like monomeric, low molecular mass GTP-binding proteins distinct from heterotrimeric G proteins such as Gi, Go and Gs are present in C. albicans.