Candida albicans homologue ofGGP1/GAS1 gene is functional inSaccharomyces cerevisiae and contains the determinants for glycosylphosphatidylinositol attachment
✍ Scribed by Vai, Marina; Orlandi, Ivan; Cavadini, Paola; Alberghina, Lilia; Popolo, Laura
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 612 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0749-503X
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✦ Synopsis
The GGPlIGASIICWH52 gene of Succhuronzyce.r cerevisiue encodes a major exocellular 1 15 kDa glycoprotein (gpll5) anchored to the plasma membrane through a glycosylphosphatidylinositol (GPI). The function of gpll5 is still unknown but the analysis of null mutants suggests a possible role in the control of morphogenesis. P H R l gene isolated from Ctindidu alibicons is homologous to the GGPl gene. In this report we have analysed the ability of P H R l to complement a ggplA mutation in S. cerevisiue. The expression of P H R l controlled by its natural promoter or by the GGPl promoter has been studied. In both cases we have observed a complete complementation of the mutant phenotype. Moreover, immunological analysis has revealed that P H R l in budding yeast gives rise to a 75-80 kDa protein anchored to the membrane through a GPI, indicating that the signal for GPI attachment present in the C. ull,icuns gene product is functional in S. cerevisirce.