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 language | English (US) |
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Pages (from-to) | 240-247 |
Number of pages | 8 |
Journal | Journal of Proteome Research |
Volume | 5 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2006 |
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
- General Chemistry