We cloned and sequenced homologs of RAS (CnRAS) and RHO1 (CnRHO1) genes fro
m Cryptococcus neoformans. The proteins encoded by the CnRAS and CnRHO1 gen
es contained 216 and 197 amino acids, respectively. The deduced amino acid
sequence of the CnRAS gene shared a high degree of sequence identity with t
he Ras proteins in other fungal species: Coprinus cinereus (76%), Lentinula
edodes (74%), Saccharomyces cerevisiae RAS2 (72%), and Schizosaccharomyces
pombe (68%). The deduced amino acid sequence of the CnRHO1 gene shared a h
igh degree of sequence identity with the Rho1 proteins in other fungal spec
ies: Candida albicans (78%), S. pombe (77%) and S. cerevisiae (76%). The de
duced proteins contained GTP-binding and GTP-hydrolysis domains, and the pr
enylation site that are conserved among the small G protein superfamily. Th
e synthetic peptides that contained the C-terminal amino acid sequence of t
he CnRas and CnRho1 proteins were geranylgeranylated. The DDBJ/EMBL/GenBank
Accession Numbers of the CnRAS and CnRHO1 genes are AB017640 and AB017639,
respectively. Copyright (C) 1999 John Wiley & Sons, Ltd.