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    A mutant O-GlcNAcase enriches Drosophila developmental regulators

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    Publication date
    2017
    Author
    Selvan, N.
    Williamson, Ritchie
    Mariappa, D.
    Campbell, D.G.
    Gourlay, R.
    Ferenbach, A.T.
    Aristotelous, T.
    Hopkins-Navratilova, I.
    Trost, M.
    van Aalten, D.M.F.
    Keyword
    O-GIcNAcase; Drosophila; Glycomics; Glycobiology; Chemical tools; Post-translational modifications
    Rights
    (c) 2017 The Authors. Full-text reproduced in accordance with the publisher self-archiving policy.
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Protein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA). Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis. Drosophila melanogaster OGT/supersex combs (sxc) is a polycomb gene, null mutants of which display homeotic transformations and die at the pharate adult stage. However, the identities of the O-GlcNAcylated proteins involved, and the underlying mechanisms linking these phenotypes to embryonic development, are poorly understood. Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and limited enrichment tools. Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, amongst others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
    URI
    http://hdl.handle.net/10454/12133
    Version
    Accepted Manuscript
    Citation
    Selvan N, Williamson R, Mariappa D et al (2017) A mutant O-GlcNAcase enriches Drosophila developmental regulators. Nature Chemical Biology. 13: 882-887.
    Link to publisher’s version
    https://doi.org/10.1038/nchembio.2404
    Type
    Article
    Collections
    Life Sciences Publications

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