An α-Amylase Homologue, aah3, Encodes a GPI-Anchored Membrane Protein Required for Cell Wall Integrity and Morphogenesis in Schizosaccharomyces pombe

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  • MORITA Tomotake
    Department of Life Sciences, Faculty of Agriculture, Kagawa University Research Center, Asahi Glass Co., Ltd.
  • TANAKA Naotaka
    Department of Life Sciences, Faculty of Agriculture, Kagawa University
  • HOSOMI Akira
    Department of Life Sciences, Faculty of Agriculture, Kagawa University
  • GIGA-HAMA Yuko
    Research Center, Asahi Glass Co., Ltd.
  • TAKEGAWA Kaoru
    Department of Life Sciences, Faculty of Agriculture, Kagawa University

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タイトル別名
  • An .ALPHA.-Amylase Homologue, aah3, Encodes a GPI-Anchored Membrane Protein Required for Cell Wall Integrity and Morphogenesis in Schizosaccharomyces pombe
  • アルファ Amylase Homologue aah3 Encodes a GPI Anchored Membrane Protein Required for Cell Wall Integrity and Morphogenesis in Schizosaccharomyces pombe
  • An α-Amylase Homologue,<i>aah3</i>, Encodes a GPI-Anchored Membrane Protein Required for Cell Wall Integrity and Morphogenesis in<i>Schizosaccharomyces pombe</i>
  • An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in <italic>Schizosaccharomyces pombe</italic>.

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Glycosylphosphatidylinositol (GPI)-anchored proteins are essential for normal cellular morphogenesis and have an additional role in mediating cross-linking of glycoproteins to cell wall glucan in yeast cells. Although many GPI-anchored proteins have been characterized in Saccharomyces cerevisiae, none have been reported for well-characterized GPI-anchored proteins in Schizosaccharomyces pombe to date. Among the putative GPI-anchored proteins in S. pombe, four α-amylase homologs (Aah1p-Aah4p) have putative signal sequences and C-terminal GPI anchor addition signals. Disruption of aah3+ resulted in a morphological defect and hypersensitivity to cell wall-degrading enzymes. Biochemical analysis showed that Aah3p is an N-glycosylated, GPI-anchored membrane protein localized in the membrane and cell wall fractions. Conjugation and sporulation were not affected by the aah3+ deletion, but the ascal wall of aah3Δ cells was easily lysed by hydrolases. Expression of aah3 alleles in which the conserved aspartic acid and glutamic acid residues required for hydrolase activity were replaced with alanine residues failed to rescue the morphological and ascal wall defects of aah3Δ cells. Taken together, these results indicate that Aah3p is a GPI-anchored protein and is required for cell and ascal wall integrity in S. pombe.

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