A mutant O-GlcNAcase enriches Drosophila developmental regulators
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2017Author
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 modificationsRights
(c) 2017 The Authors. Full-text reproduced in accordance with the publisher self-archiving policy.Peer-Reviewed
Yes
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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.Version
Accepted ManuscriptCitation
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 Version of Record
https://doi.org/10.1038/nchembio.2404Type
Articleae974a485f413a2113503eed53cd6c53
https://doi.org/10.1038/nchembio.2404