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

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

Research output: Contribution to journalArticle

Abstract

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
Volume5
Issue number2
DOIs
StatePublished - Feb 1 2006

Fingerprint

S 10
Acetylation
Methylation
Colchicine
HeLa Cells
Histones
Mass spectrometry
Mass Spectrometry
Cells
Electrons
Proteins

Keywords

  • 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)

Cite this

Mass spectrometric characterization of human histone H3 : A bird's eye view. / Thomas, C. Eric; Kelleher, Neil L.; Mizzen, Craig A.

In: Journal of Proteome Research, Vol. 5, No. 2, 01.02.2006, p. 240-247.

Research output: Contribution to journalArticle

Thomas, C. Eric ; Kelleher, Neil L. ; Mizzen, Craig A. / Mass spectrometric characterization of human histone H3 : A bird's eye view. In: Journal of Proteome Research. 2006 ; Vol. 5, No. 2. pp. 240-247.
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