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Methods Mol Biol. 2009;534:251-79. doi: 10.1007/978-1-59745-022-5_19.

Detecting the "O-GlcNAc-ome"; detection, purification, and analysis of O-GlcNAc modified proteins.

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1
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. nzachara@jhmi.edu

Abstract

The modification of Ser and Thr residues of cytoplasmic and nuclear proteins with a monosaccharide of O-linked beta-N-acetylglucosamine is an essential and dynamic post-translational modification of metazoans. Deletion of the O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc, is lethal in mammalian cells highlighting the importance of this post-translational modification in regulating cellular function. O-GlcNAc is believed to modulate protein function in a manner analogous to protein phosphorylation. Notably, on some proteins O-GlcNAc and O-phosphate modify the same Ser/Thr residue, suggesting that a reciprocal relationship exists between these two post-translational modifications. In this chapter we describe the most robust techniques for the detection and purification of O-GlcNAc modified proteins, and discuss some more specialized techniques for site-mapping and detection of O-GlcNAc during mass spectrometry.

PMID:
19277546
DOI:
10.1007/978-1-59745-022-5_19
[Indexed for MEDLINE]
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