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dc.contributor.authorSelvan, N.*
dc.contributor.authorWilliamson, Ritchie*
dc.contributor.authorMariappa, D.*
dc.contributor.authorCampbell, D.G.*
dc.contributor.authorGourlay, R.*
dc.contributor.authorFerenbach, A.T.*
dc.contributor.authorAristotelous, T.*
dc.contributor.authorHopkins-Navratilova, I.*
dc.contributor.authorTrost, M.*
dc.contributor.authorvan Aalten, D.M.F.*
dc.date.accessioned2017-06-06T15:57:32Z
dc.date.available2017-06-06T15:57:32Z
dc.date.issued2017
dc.identifier.citationSelvan N, Williamson R, Mariappa D et al (2017) A mutant O-GlcNAcase enriches Drosophila developmental regulators. Nature Chemical Biology. 13: 882-887.en_US
dc.identifier.urihttp://hdl.handle.net/10454/12133
dc.descriptionYesen_US
dc.description.abstractProtein 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.en_US
dc.description.sponsorshipWellcome Trust Investigator Award (110061); MRC grant (MC_UU_12016/5); and Royal Society Research Grant.
dc.language.isoenen_US
dc.relation.isreferencedbyhttps://doi.org/10.1038/nchembio.2404
dc.rights(c) 2017 The Authors. Full-text reproduced in accordance with the publisher self-archiving policy.
dc.subjectO-GIcNAcase; Drosophila; Glycomics; Glycobiology; Chemical tools; Post-translational modificationsen_US
dc.titleA mutant O-GlcNAcase enriches Drosophila developmental regulatorsen_US
dc.status.refereedYesen_US
dc.date.Accepted2017-03-14
dc.date.application2017-06-12
dc.typeArticleen_US
dc.type.versionAccepted Manuscripten_US
refterms.dateFOA2017-12-13T00:00:00Z


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