GSBS Student Publications

Title

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

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine

Date

4-13-2005

Document Type

Article

Medical Subject Headings

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

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: Curr Biol. 2005 Apr 12;15(7):656-60. Link to article on publisher's site

DOI of Published Version

10.1016/j.cub.2005.02.049

Related Resources

Link to article in PubMed

Journal Title

Current biology : CB

PubMed ID

15823538