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J Biol Chem. 1998 Oct 9;273(41):26946-53.

Amino acid sequence requirement for efficient incorporation of glycosylphosphatidylinositol-associated proteins into the cell wall of Saccharomyces cerevisiae.

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  • 1Department of Mycology, Nippon Roche Research Center, Kamakura, Kanagawa 247, Japan.


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.

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