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    Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase

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    Authors
    Silberstein, Susana
    Gilmore, Reid
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Biology
    Document Type
    Journal Article
    Publication Date
    1996-06-01
    Keywords
    Animals
    Carbohydrate Sequence
    Forecasting
    Glycosylation
    *Hexosyltransferases
    Humans
    *Membrane Proteins
    Molecular Sequence Data
    Phenotype
    Saccharomyces cerevisiae
    Transferases
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://doi.org/10.1096/fasebj.10.8.8666161
    Abstract
    Asparagine-linked glycosylation is a highly conserved protein modification reaction that occurs in all eukaryotes. The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum. Biochemical, molecular biological, and genetic studies conducted during the past 5 years have resulted in an explosive growth in our knowledge concerning the OST. Although the basic biochemical properties of the enzyme were determined more than a decade ago using intact microsomal membranes, recent studies provide novel insight into the catalytic mechanism of the enzyme. The OST was recently purified as a large heteroligomeric membrane protein complex; the sequences of many of the subunits have been determined from both fungal and vertebrate sources. Consistent with the evolutionary conservation of N-linked glycosylation, protein sequence comparisons reveal significant homologies between vertebrate, invertebrate, plant, and fungal OST subunits. Yeast molecular genetic methods have been instrumental in the functional characterization of the OST subunits, and have proven to be powerful tools for the identification of novel gene products that influence oligosaccharide transfer in vivo.
    Source

    FASEB J. 1996 Jun;10(8):849-58.

    DOI
    10.1096/fasebj.10.8.8666161
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42198
    PubMed ID
    8666161
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1096/fasebj.10.8.8666161
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    UMass Chan Faculty and Researcher Publications

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