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Nucleic Acids Res. 2011 Aug;39(15):6465-74. doi: 10.1093/nar/gkr304. Epub 2011 May 16.

Phosphorylation of histone H3(T118) alters nucleosome dynamics and remodeling.

Author information

1
Department of Physics, The Ohio State University and The Ohio State University Medical Center, Columbus, OH 43210, USA.

Abstract

Nucleosomes, the fundamental units of chromatin structure, are regulators and barriers to transcription, replication and repair. Post-translational modifications (PTMs) of the histone proteins within nucleosomes regulate these DNA processes. Histone H3(T118) is a site of phosphorylation [H3(T118ph)] and is implicated in regulation of transcription and DNA repair. We prepared H3(T118ph) by expressed protein ligation and determined its influence on nucleosome dynamics. We find H3(T118ph) reduces DNA-histone binding by 2  kcal/mol, increases nucleosome mobility by 28-fold and increases DNA accessibility near the dyad region by 6-fold. Moreover, H3(T118ph) increases the rate of hMSH2-hMSH6 nucleosome disassembly and enables nucleosome disassembly by the SWI/SNF chromatin remodeler. These studies suggest that H3(T118ph) directly enhances and may reprogram chromatin remodeling reactions.

PMID:
21576235
PMCID:
PMC3159469
DOI:
10.1093/nar/gkr304
[Indexed for MEDLINE]
Free PMC Article

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