title: The cell cycle modulated glycoprotein GP115 is one of the major yeast proteins containing glycosylphosphatidylinositol.
abstract: The cell cycle modulated protein gp115 (115 kDa, isoelectric point about 4.8-5) of Saccharomyces cerevisiae undergoes various post-translational modifications. It is N-glycosylated during its maturation along the secretory pathway where an intermediary precursor of 100 kDa (p100), dynamically related to the mature gp115 protein, is detected at the level of endoplasmic reticulum. Moreover, we have shown by the use of metabolic labeling with [35S]methionine, [3H]palmitic acid and myo-[3H]inositol combined with high resolution two-dimensional gel electrophoresis and immunoprecipitation with a specific antiserum, that gp115 is one of the major palmitate- and inositol-containing proteins in yeast. These results, and the susceptibility of gp115 to phosphatidylinositol-specific phospholipase C treatment strongly indicate that gp115 contains the glycosylphosphatidylinositol (GPI) structure as membrane anchor domain. The two-dimensional analysis of the palmitate- and inositol-labeled proteins has also allowed the characterization of other polypeptides which possibly contain a GPI structure.
authors.affiliation: Dipartimento di Fisiologia e Biochimica Generali, Università di Milano, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Vai
authors.forename: L
authors.initials: L
authors.lastname: Popolo
authors.forename: R
authors.initials: R
authors.lastname: Grandori
authors.forename: E
authors.initials: E
authors.lastname: Lacanà
authors.forename: L
authors.initials: L
authors.lastname: Alberghina
mesh_terms: D000118:Acetylglucosaminidase; D002453:Cell Cycle; D015180:Electrophoresis, Gel, Two-Dimensional; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D006017:Glycolipids / Q000235:genetics / Q000378:metabolism*; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D017261:Glycosylphosphatidylinositols; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000235:genetics / Q000378:metabolism*; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D006017:Glycolipids; D006023:Glycoproteins; D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D010169:Palmitic Acids; D010716:Phosphatidylinositols; D019308:Palmitic Acid; D008715:Methionine; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D043265:Phosphatidylinositol Diacylglycerol-Lyase