Abstract
Cell wall proteins of Saccharomyces cerevisiae are anchored by means of a beta-1, 6-glucan-containing side-chain. It is not known whether this chain is linked to the protein part (e.g. through carbohydrate side-chains) or to the glycosylphosphatidylinositol (GPI) moiety of cell wall proteins. An IgA protease recognition site was introduced in Cwp2p, a beta-1, 6-glucosylated cell wall protein, immediately N-terminal from the omega amino acid (the attachment site of the GPI moiety). Proteolytic cleavage of this site revealed that the beta-1, 6-glucan epitope was not linked to the protein part. We conclude that neither N-or O-glycosylation is involved in beta-glucosylation of cell wall proteins. This confirms that the glycan core of the GPI moiety is the probable beta-1, 6-glucan attachment site.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blotting, Western
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Carbohydrate Sequence
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Cell Wall / enzymology
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Genes, Reporter / physiology
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Glucans / chemistry
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Glucans / metabolism*
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Glycosylation
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Glycosylphosphatidylinositols / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Polysaccharides / metabolism
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae / enzymology*
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Serine Endopeptidases / metabolism
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Transformation, Genetic
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alpha-Galactosidase / metabolism
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beta-Glucans*
Substances
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Fungal Proteins
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Glucans
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Glycosylphosphatidylinositols
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Membrane Proteins
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Polysaccharides
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beta-Glucans
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beta-1,6-glucan
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alpha-Galactosidase
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Serine Endopeptidases
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IgA-specific serine endopeptidase