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    The alpha subunit of the Saccharomyces cerevisiae oligosaccharyltransferase complex is essential for vegetative growth of yeast and is homologous to mammalian ribophorin I

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    Authors
    Silberstein, Susana
    Collins, Pallia G.
    Kelleher, Daniel J.
    Rapiejko, Peter J.
    Gilmore, Reid
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Biology
    Document Type
    Journal Article
    Publication Date
    1995-02-01
    Keywords
    Amino Acid Sequence
    Asparagine
    Base Sequence
    Fungal Proteins
    Genes, Fungal
    Genes, Lethal
    Genomic Library
    Glycosylation
    HSP70 Heat-Shock Proteins
    *Hexosyltransferases
    Membrane Proteins
    Microsomes
    Molecular Sequence Data
    Mutagenesis
    Oligosaccharides
    Protein Conformation
    Protein Processing, Post-Translational
    Saccharomyces cerevisiae
    Sequence Analysis, DNA
    Sequence Homology, Amino Acid
    Transferases
    Biochemistry
    Cell Biology
    Molecular Biology
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    Abstract
    Oligosaccharyltransferase mediates the transfer of a preassembled high mannose oligosaccharide from a lipid-linked oligosaccharide donor to consensus glycosylation acceptor sites in newly synthesized proteins in the lumen of the rough endoplasmic reticulum. The Saccharomyces cerevisiae oligosaccharyltransferase is an oligomeric complex composed of six nonidentical subunits (alpha-zeta), two of which are glycoproteins (alpha and beta). The beta and delta subunits of the oligosaccharyltransferase are encoded by the WBP1 and SWP1 genes. Here we describe the functional characterization of the OST1 gene that encodes the alpha subunit of the oligosaccharyltransferase. Protein sequence analysis revealed a significant sequence identity between the Saccharomyces cerevisiae Ost1 protein and ribophorin I, a previously identified subunit of the mammalian oligosaccharyltransferase. A disruption of the OST1 locus was not tolerated in haploid yeast showing that expression of the Ost1 protein is essential for vegetative growth of yeast. An analysis of a series of conditional ost1 mutants demonstrated that defects in the Ost1 protein cause pleiotropic underglycosylation of soluble and membrane-bound glycoproteins at both the permissive and restrictive growth temperatures. Microsomal membranes isolated from ost1 mutant yeast showed marked reductions in the in vitro transfer of high mannose oligosaccharide from exogenous lipid-linked oligosaccharide to a glycosylation site acceptor tripeptide. Microsomal membranes isolated from the ost1 mutants contained elevated amounts of the Kar2 stress-response protein.
    Source
    J Cell Biol. 1995 Feb;128(4):525-36.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42617
    PubMed ID
    7860628
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