Yes / 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. / Wellcome Trust Investigator Award (110061); MRC grant (MC_UU_12016/5); and Royal Society Research Grant.
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/12133 |
| Date | 12 June 2017 |
| Creators | 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. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, Accepted Manuscript |
| Rights | (c) 2017 The Authors. Full-text reproduced in accordance with the publisher self-archiving policy. |
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