Journal
EPIGENETICS
Volume 10, Issue 8, Pages 677-691Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15592294.2015.1060387
Keywords
Chromatin; Epigenetics; Histone; HCF-1; OGT; O-GlcNAc; O-GlcNAcylation; Polycomb; posttranslational modification; TET2
Funding
- Canadian Institutes of Health Research (CIHR) [MOP-115132]
- Natural Sciences and Engineering Research Council of Canada (NSERC) [355814-2010, 435636-2013]
- FRQ-S
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O-GlcNAcylation is a posttranslational modification catalyzed by the O-Linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and reversed by O-GlcNAcase (OGA). Numerous transcriptional regulators, including chromatin modifying enzymes, transcription factors, and co-factors, are targeted by O-GlcNAcylation, indicating that this modification is central for chromatin-associated processes. Recently, OGT-mediated O-GlcNAcylation was reported to be a novel histone modification, suggesting a potential role in directly coordinating chromatin structure and function. In contrast, using multiple biochemical approaches, we report here that histone O-GlcNAcylation is undetectable in mammalian cells. Conversely, O-GlcNAcylation of the transcription regulators Host Cell Factor-1 (HCF-1) and Ten-Eleven Translocation protein 2 (TET2) could be readily observed. Our study raises questions on the occurrence and abundance of O-GlcNAcylation as a histone modification in mammalian cells and reveals technical complications regarding the detection of genuine protein O-GlcNAcylation. Therefore, the identification of the specific contexts in which histone O-GlcNAcylation might occur is still to be established.
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