CANDIDA-ALBICANS HOMOLOG OF GGP1 GAS1 GENE IS FUNCTIONAL IN SACCHAROMYCES-CEREVISIAE AND CONTAINS THE DETERMINANTS FOR GLYCOSYLPHOSPHATIDYLINOSITOL ATTACHMENT/

The GGP1/GAS1/CWH52 gene of Saccharomyces cerevisiae encodes a major e xocellular 115 kDa glycoprotein (gp115) anchored to the plasma membran e through a glycosylphosphatidylinositol (GPI). The function of gp115 is still unknown but the analysis of null mutants suggests a possible role in the control of morphogenesis. PHR1 gene isolated from Candida alibicans is homologous to the GGP1 gene. In this report we have analy sed the ability of PHR1 to complement a ggpI Delta mutation in S. cere visiae. The expression of PHR1 controlled by its natural promoter or b y the GGP1 promoter has been studied. In both cases we have observed a complete complementation of the mutant phenotype. Moreover, immunolog ical analysis has revealed that PHR1 in budding yeast gives rise to a 75-80 kDa protein anchored to the membrane through a GPI, indicating t hat the signal for GPI attachment present in the C. albicans gene prod uct is functional in S. cerevisiae.