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Epigenetics. 2013 Oct;8(10):1101-13. doi: 10.4161/epi.26025. Epub 2013 Aug 15.

Initial characterization of histone H3 serine 10 O-acetylation.

Author information

1
Department of Molecular Biology; Princeton University; Princeton, NJ USA; Epigenetics Program; Department of Biochemistry and Biophysics; Perelman School of Medicine; University of Pennsylvania; Philadelphia, PA USA.
2
Molecular and Cellular Oncogenesis Program; The Wistar Institute; Philadelphia, PA USA.
3
Epigenetics Program; Department of Biochemistry and Biophysics; Perelman School of Medicine; University of Pennsylvania; Philadelphia, PA USA.
4
University of California Los Angeles; David Geffen School of Medicine; Department of Biological Chemistry; Jonsson Comprehensive Cancer Center; Molecular Biology Institute; Bioinformatics Interdepartmental Degree Program; Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research; Los Angeles, CA USA; Current affiliation: Wisconsin Institute for Discovery; Department of Cell and Regenerative Biology; University of Wisconsin; Madison, WI USA.
5
University of California Los Angeles; David Geffen School of Medicine; Department of Biological Chemistry; Jonsson Comprehensive Cancer Center; Molecular Biology Institute; Bioinformatics Interdepartmental Degree Program; Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research; Los Angeles, CA USA.

Abstract

In eukaryotic organisms, histone posttranslational modifications (PTMs) are indispensable for their role in maintaining cellular physiology, often through their mediation of chromatin-related processes such as transcription. Targeted investigations of this ever expanding network of chemical moieties continue to reveal genetic, biochemical, and cellular nuances of this complex landscape. In this study, we present our findings on a novel class of histone PTMs: Serine, Threonine, and Tyrosine O-acetylation. We have combined highly sensitive nano-LC-MS/MS experiments and immunodetection assays to identify and validate these unique marks found only on histone H3. Mass spectrometry experiments have determined that several of these O-acetylation marks are conserved in many species, ranging from yeast to human. Additionally, our investigations reveal that histone H3 serine 10 acetylation (H3S10ac) is potentially linked to cell cycle progression and cellular pluripotency. Here, we provide a glimpse into the functional implications of this H3-specific histone mark, which may be of high value for further studies of chromatin.

KEYWORDS:

chromatin; epigenetics; histone; mass spectrometry; post-translational modifications; proteomics; quantitative; stem cells

PMID:
23949383
PMCID:
PMC3891691
DOI:
10.4161/epi.26025
[Indexed for MEDLINE]
Free PMC Article
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