ArticleThe Journal of biological chemistry2011
Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 130 citations in OpenAlex.
- Nuclear N-glycosylation maintains H3K9me3 heterochromatin and genomic stability.Nature cell biology · 2026Article
- Protein O-GlcNAcylation in Health and Diseases.MedComm · 2025Review
- O-GlcNAcylation of nuclear proteins in the mouse liver exhibit daily oscillations that are influenced by meal timing.PLoS biology · 2025Article
- Mealtime alters daily rhythm in nuclear O-GlcNAc proteome to regulate hepatic gene expression.bioRxiv : the preprint server for biology · 2025Article
- Role of histone post-translational modifications in atherosclerosis and the therapeutic potential of targeting epigenetic modifiers.Frontiers in cell and developmental biology · 2025Review
- Direct radical functionalization of native sugars.Nature · 2024Article
- Approaches to the Full and Partial Chemical Synthesis of Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- O-GlcNAcylation: the sweet side of epigenetics.Epigenetics & chromatin · 2023Review
- The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023Review
- H4S47 O-GlcNAcylation regulates the activation of mammalian replication origins.Nature structural & molecular biology · 2023Article
- Epimutations and Their Effect on Chromatin Organization: Exciting Avenues for Cancer Treatment.Cancers · 2022Review
- Investigation of in vitro histone H3 glycosylation using H3 tail peptides.Scientific reports · 2022Article
- An Epigenetic Role of Mitochondria in Cancer.Cells · 2022Review
- Unconventional metabolites in chromatin regulation.Bioscience reports · 2022Article
- O-GlcNAcylation links oncogenic signals and cancer epigenetics.Discover oncology · 2021Review
- The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.Genes · 2021Review
- Role ofPhysiological reviews · 2021Review
- Feedback Regulation ofInternational journal of molecular sciences · 2021Article
- Overview of the Assays to ProbeMolecules (Basel, Switzerland) · 2021Review
- C-Terminal Tag Location Hampers in Vitro Profiling of OGT Peptide Substrates by mRNA Display.Chembiochem : a European journal of chemical biology · 2021Article
23 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci. STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022). This post-translational protein modification, termed O-GlcNAcylation, is reversible, analogous to phosphorylation, and has been implicated in many cellular processes. Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A. Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph). Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc). Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones. We also examined histone O-GlcNAcylation during cell cycle progression. Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis. Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
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