Initial characterization of histone H3 serine 10 O-acetylation

Laura Mae P. Britton, Alyshia Newhart, Natarajan V. Bhanu, Rupa Sridharan, Michelle Gonzales-Cope, Kathrin Plath, Susan M. Janicki, Benjamin A. Garcia

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


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.

Original languageEnglish
Pages (from-to)1101-1113
Number of pages13
Issue number10
StatePublished - Oct 2013


  • Chromatin
  • Epigenetics
  • Histone
  • Mass spectrometry
  • Post-translational modifications
  • Proteomics
  • Quantitative
  • Stem cells


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