Journal
JOURNAL OF PROTEOME RESEARCH
Volume 5, Issue 2, Pages 240-247Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr050266a
Keywords
H3; histone code; histone-Fourier transform mass spectrometry (FTMS); electron capture dissociation (ECD); chromatin; post-translational modification (PTM); acetylation; methylation; phosphorylation
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Funding
- NIGMS NIH HHS [GM 067193] Funding Source: Medline
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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 similar to 5% methylation of K4 and similar to 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 similar to+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.
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