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Phosphorylation of histone H4 serine 1 during DNA damage requires casein kinase II in S. cerevisiae.

Distinct patterns of posttranslational histone modifications can regulate DNA-templated events such as mitosis, transcription, replication, apoptosis, and DNA damage, suggesting the presence of a "histone code" in these nuclear processes. Phosphorylation of histone H2A S129 at sites of DNA double-strand breaks (DSBs) has been implicated in damage repair in yeast. Here, we describe another phosphorylation event on serine 1 (S1) of histone H4; this event is also associated with MMS- or phleomycin-induced DSBs but not with UV-induced DNA damage. Chromatin-immunoprecipitation (ChIP) studies of an HO-endonuclease-inducible strain show that S1 phosphorylation is specifically enhanced 20- to 25-fold in nucleosomes proximal to the DSB. In addition, we show that casein kinase II (CK2) can phosphorylate H4 S1 in vitro and that null or temperature-sensitive CK2 yeast mutants are defective for induction of H4 S1 phosphorylation upon DNA damage in vivo. Furthermore, H4 S1 phosphorylation and CK2 play a role in DSB re-joining as indicated by a nonhomologous end-joining (NHEJ) plasmid assay. CK2 has been implicated in regulating a DNA-damage response; our data suggest that histone H4 S1 is one of its physiological substrates. These data suggest that this modification is a part of the DNA-repair histone code.

Pubmed ID: 15823538


  • Cheung WL
  • Turner FB
  • Krishnamoorthy T
  • Wolner B
  • Ahn SH
  • Foley M
  • Dorsey JA
  • Peterson CL
  • Berger SL
  • Allis CD


Current biology : CB

Publication Data

April 12, 2005

Associated Grants

  • Agency: NIGMS NIH HHS, Id: 1 F32 GM64233
  • Agency: NCI NIH HHS, Id: CA82834
  • Agency: NIGMS NIH HHS, Id: GM40922

Mesh Terms

  • Blotting, Western
  • Casein Kinase II
  • Chromatin Immunoprecipitation
  • DNA Damage
  • DNA Repair
  • Histones
  • Nucleosomes
  • Phosphorylation
  • Saccharomyces cerevisiae
  • Serine