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    The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases

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    Authors
    Samuelson, John
    Banerjee, Sulagna
    Magnelli, Paula
    Cui, Jike
    Kelleher, Daniel J.
    Gilmore, Reid
    Robbins, Phillips W.
    UMass Chan Affiliations
    Biochemistry and Molecular Pharmacology
    Neurobiology
    Document Type
    Journal Article
    Publication Date
    2005-02-01
    Keywords
    Animals
    *Asparagine
    Bacteria
    Computational Biology
    Dolichol
    Evolution, Molecular
    *Genetic Variation
    Glycopeptides
    Glycosyltransferases
    Humans
    Polysaccharides
    Species Specificity
    Biochemistry
    Biochemistry, Biophysics, and Structural Biology
    Bioinformatics
    Molecular Biology
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    Link to Full Text
    http://dx.doi.org/10.1073/pnas.0409460102
    Abstract
    The vast majority of eukaryotes (fungi, plants, animals, slime mold, and euglena) synthesize Asn-linked glycans (Alg) by means of a lipid-linked precursor dolichol-PP-GlcNAc2Man9Glc3. Knowledge of this pathway is important because defects in the glycosyltransferases (Alg1-Alg12 and others not yet identified), which make dolichol-PP-glycans, lead to numerous congenital disorders of glycosylation. Here we used bioinformatic and experimental methods to characterize Alg glycosyltransferases and dolichol-PP-glycans of diverse protists, including many human pathogens, with the following major conclusions. First, it is demonstrated that common ancestry is a useful method of predicting the Alg glycosyltransferase inventory of each eukaryote. Second, in the vast majority of cases, this inventory accurately predicts the dolichol-PP-glycans observed. Third, Alg glycosyltransferases are missing in sets from each organism (e.g., all of the glycosyltransferases that add glucose and mannose are absent from Giardia and Plasmodium). Fourth, dolichol-PP-GlcNAc2Man5 (present in Entamoeba and Trichomonas) and dolichol-PP- and N-linked GlcNAc2 (present in Giardia) have not been identified previously in wild-type organisms. Finally, the present diversity of protist and fungal dolichol-PP-linked glycans appears to result from secondary loss of glycosyltransferases from a common ancestor that contained the complete set of Alg glycosyltransferases.
    Source
    Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1548-53. Epub 2005 Jan 21. Link to article on publisher's site
    DOI
    10.1073/pnas.0409460102
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/26045
    PubMed ID
    15665075
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.0409460102
    Scopus Count
    Collections
    UMass Chan Faculty and Researcher Publications
    Neurobiology Faculty Publications

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