NDLI: Phosphorylation of Histone H2B at DNA Double-Strand Breaks

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Phosphorylation of Histone H2B at DNA Double-Strand Breaks

Content Provider	Semantic Scholar
Author	Fernández-Capetillo, Oscar Allis, C. David Nussenzweig, André
Copyright Year	2004
Abstract	Posttranslational modifications of histone tails regulate numerous biological processes including transcription, DNA repair, and apoptosis. Although recent studies suggest that structural alterations in chromatin are critical for triggering the DNA damage response, very little is known about the nature of DNA damage-induced chromatin perturbations. Here we show that the serine 14 residue in the NH(2)-terminal tail of histone H2B is rapidly phosphorylated at sites of DNA double-strand breaks. At late time points after irradiation, the phosphorylated form of H2B, H2B-(Ser14P), accumulates into irradiation-induced foci. H2B-(Ser14P) foci formation is not associated with the apoptotic phosphorylation of H2B but is strictly dependent on the phosphorylated isoform of H2AX. Our results broaden the spectrum of histone modifications that constitute the DNA damage "histone code" and suggest a model for the underlying chromatin structure within damage-induced foci.
Starting Page	1671
Ending Page	1677
Page Count	7
File Format	PDF HTM / HTML
PubMed reference number	15197225
Volume Number	199
Journal	The Journal of experimental medicine
Alternate Webpage(s)	http://jem.rupress.org/content/jem/199/12/1671.full.pdf?with-ds=yes
Alternate Webpage(s)	http://jem.rupress.org/content/jem/199/12/1671.full.pdf
Alternate Webpage(s)	http://ftp.ncbi.nlm.nih.gov/pub/pmc/69/ca/20032247.PMC2212807.pdf
Language	English
Access Restriction	Open
Subject Keyword	Apoptosis DNA Damage DNA Repair H2AX protein, human Histone Code Histone H2b Histones Post-Translational Protein Processing Tail
Content Type	Text
Resource Type	Article

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