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Lookup NU author(s): Robert Gourlay, Professor Matthias TrostORCiD
This is the final published version of an article that has been published in its final definitive form by Nature Publishing Group, 2017.
For re-use rights please refer to the publisher's terms and conditions.
© 2017 Nature America, Inc., part of Springer Nature. All rights reserved. Protein O-GlcNAcylation is a reversible post-translational modification of serines and 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. The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants 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 by 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, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
Author(s): Selvan N, Williamson R, Mariappa D, Campbell DG, Gourlay R, Ferenbach AT, Aristotelous T, Hopkins-Navratilova I, Trost M, Van Aalten DMF
Publication type: Article
Publication status: Published
Journal: Nature Chemical Biology
Year: 2017
Volume: 13
Issue: 8
Pages: 882-887
Online publication date: 12/06/2017
Acceptance date: 14/03/2017
Date deposited: 23/08/2018
ISSN (print): 1552-4450
ISSN (electronic): 1552-4469
Publisher: Nature Publishing Group
URL: https://doi.org/10.1038/nchembio.2404
DOI: 10.1038/nchembio.2404
PubMed id: 28604694
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