Abstract
Glycosylphosphatidylinositol (GPI) anchors are added onto newly synthesized proteins in the ER. Thereby a putative transamidase removes a C-terminal peptide and attaches the truncated protein to the free amino group of the preformed GPI. The yeast mutant gpi8-1 is deficient in this addition of GPIs to proteins. GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. GPI8 shows significant homology to a novel family of vacuolar plant endopeptidases one of which is supposed to catalyse a transamidation step in the maturation of concanavalin A and acts as a transamidase in vitro. Humans have a gene which is highly homologous to GPI8 and can functionally replace it.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aminoacyltransferases
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Animals
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Cell Adhesion Molecules / biosynthesis
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / metabolism*
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Genes, Fungal
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Glycosylation
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Glycosylphosphatidylinositols / metabolism*
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Humans
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Molecular Sequence Data
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Plants
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Polymerase Chain Reaction
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / growth & development
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Schistosoma
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Sequence Homology, Amino Acid
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Sequence Tagged Sites
Substances
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Cell Adhesion Molecules
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Glycosylphosphatidylinositols
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PIGK protein, human
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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Aminoacyltransferases
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GPI8 protein, S cerevisiae