The GGP1/GAS1/CWH52 gene of Saccharomyces cerevisiae encodes a major exocellular 115 kDa glycoprotein (gp115) anchored to the plasma membrane 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 analysed the ability of PHR1 to complement a ggp1 delta mutation in S. cerevisiae. The expression of PHR1 controlled by its natural promoter or by the GGP1 promoter has been studied. In both cases we have observed a complete complementation of the mutant phenotype. Moreover, immunological analysis has revealed that PHR1 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. albicans gene product is functional in S. cerevisiae

Vai, M., Orlandi, I., Cavadini, P., Alberghina, L., Popolo, L. (1996). Candida albicans homologue of GGP1/GAS1 gene is functional in Saccharomyces cerevisiae and contains the determinants for glycosylphosphatidylinositol attachment. YEAST, 12(4), 361-368 [10.1002/(SICI)1097-0061(19960330)12:4<361::AID-YEA920>3.0.CO;2-T].

Candida albicans homologue of GGP1/GAS1 gene is functional in Saccharomyces cerevisiae and contains the determinants for glycosylphosphatidylinositol attachment

VAI, MARINA
Primo
;
ORLANDI, IVAN
Secondo
;
ALBERGHINA, LILIA
Penultimo
;
1996

Abstract

The GGP1/GAS1/CWH52 gene of Saccharomyces cerevisiae encodes a major exocellular 115 kDa glycoprotein (gp115) anchored to the plasma membrane 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 analysed the ability of PHR1 to complement a ggp1 delta mutation in S. cerevisiae. The expression of PHR1 controlled by its natural promoter or by the GGP1 promoter has been studied. In both cases we have observed a complete complementation of the mutant phenotype. Moreover, immunological analysis has revealed that PHR1 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. albicans gene product is functional in S. cerevisiae
Articolo in rivista - Articolo scientifico
Base Sequence; Blotting, Northern; Candida albicans; Fungal Proteins; Genetic Complementation Test; Glycosylphosphatidylinositols; Membrane Glycoproteins; Molecular Sequence Data; Saccharomyces cerevisiae; Genes, Fungal; Saccharomyces cerevisiae Proteins
English
361
368
8
Vai, M., Orlandi, I., Cavadini, P., Alberghina, L., Popolo, L. (1996). Candida albicans homologue of GGP1/GAS1 gene is functional in Saccharomyces cerevisiae and contains the determinants for glycosylphosphatidylinositol attachment. YEAST, 12(4), 361-368 [10.1002/(SICI)1097-0061(19960330)12:4<361::AID-YEA920>3.0.CO;2-T].
Vai, M; Orlandi, I; Cavadini, P; Alberghina, L; Popolo, L
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/59372
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