The Journal of Experimental Medicine
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Published online 14 June 2004 doi:10.1084/jem.20032247
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 199, Number 12, 1671-1677
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Phosphorylation of Histone H2B at DNA Double-Strand Breaks

Oscar Fernandez-Capetillo1, C. David Allis2, and André Nussenzweig1

1 Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892
2 Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10021

Address correspondence to André Nussenzweig, NCI/NIH Bldg. 10/4B04, 10 Center Dr., Bethesda, MD 20892. Phone: (301) 435-6425; Fax: (301) 496-0887; email: andre_nussenzweig{at}nih.gov

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 NH2-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.

Key Words: DNA damage • epigenetics • histone H2B • chromatin • histone code

The online version of this article contains supplemental material.

Abbreviations used in this paper: ATM, ataxia-telangiectasia mutated; DAPI: 4',6'-diamidino-2-phe-nylindole; DSB, double-strand break; IR, ionizing radiation; IRIF, ionizing radiation-induced foci; MEF, mouse embryonic fibroblast; PIKK, phosphatidylinositol 3-OH–kinase–related kinase.


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