Author(s): Tanaka K, Nambu H, Katoh Y, Kai M, Hidaka Y
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Abstract We cloned and sequenced homologs of RAS(CnRAS) and RHO1(CnRHO1) genes from Cryptococcus neoformans. The proteins encoded by the CnRAS and CnRHO1 genes contained 216 and 197 amino acids, respectively. The deduced amino acid sequence of the CnRAS gene shared a high degree of sequence identity with the 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 high degree of sequence identity with the Rho1 proteins in other fungal species: Candida albicans(78\%), S. pombe(77\%) and S. cerevisiae(76\%). The deduced proteins contained GTP-binding and GTP-hydrolysis domains, and the prenylation site that are conserved among the small G protein superfamily. The synthetic peptides that contained the C-terminal amino acid sequence of the CnRas and CnRho1 proteins were geranylgeranylated. Copyright 1999 John Wiley & Sons, Ltd.
This article was published in Yeast
and referenced in Fungal Genomics & Biology