Amino acid sequence requirement for efficient incorporation of glycosylphosphatidylinositol-associated proteins into the cell wall of Saccharomyces cerevisiae.
During cell wall biogenesis in Saccharomyces cerevisiae, some glycosylphosphatidylinositol (GPI)-attached proteins are detached from GPI moieties and bound to beta-1,6-glucan of the cell wall. The amino acid sequence requirement for the incorporation of GPI-attached proteins into the cell wall was studied by using reporter fusion proteins. Only the short omega-minus region composed of five amino acids, which is located upstream of the omega site for GPI attachment, determined the cellular localization of the GPI-associated proteins. Within the omega-minus region, amino acid residues at the omega-4 or -5 and omega-2 sites were important for the cell wall incorporation. Yap3p, a well characterized GPI-anchored plasma membrane aspartic protease, was localized in the cell wall when the omega-minus region was mutated to sequences containing Val or Ile at the omega-4 or -5 site and Val or Tyr at the omega-2 site.
Department of Mycology, Nippon Roche Research Center, Kamakura, Kanagawa 247, Japan.
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Hamada
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Terashima
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Arisawa
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Kitada
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases; C499266:YPS1 protein, S cerevisiae