Mass spectrometric characterization of human histone H3: A bird's eye view

C. Eric Thomas, Neil L. Kelleher, Craig A. Mizzen*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

166 Scopus citations


The modification of H3 in asynchronous HeLa cells was profiled using Top Down Mass Spectrometry. A broad distribution of species differing by 14 Da and containing less than 3% unmodified protein was observed for all three variants. Species of up to +168 Da were observed for H3.1, and fragmentation of all species by Electron Capture Dissociation (ECD) revealed ∼5% methylation of K4 and ∼50% dimethylation of K9. K14 and K23 were major sites of acetylation. H3.3 was slightly hypermodified with the apex of the distribution shifted by ∼+14 Da compared to H3.1. H3.1 (50% and 15%) from colchicine-treated cells was monophosphorylated and diphosphorylated, respectively, with equivalent modification of S10 and S28.

Original languageEnglish (US)
Pages (from-to)240-247
Number of pages8
JournalJournal of Proteome Research
Issue number2
StatePublished - Feb 2006


  • Acetylation
  • Chromatin
  • Electron capture dissociation (ECD)
  • Fourier transform mass spectrometry (FTMS)
  • H3
  • Histone
  • Histone code
  • Methylation
  • Phosphorylation
  • Post-translational modification (ptm)

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)


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