Phosphorylation of histone H4 serine 1 during DNA damage requires casein kinase II in S. cerevisiae
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Authors
Cheung, Wang L.Turner, Fiona B.
Krishnamoorthy, Thanuja
Wolner, Branden
Ahn, Sung-Hee
Foley, Melissa Anne
Dorsey, Jean A.
Peterson, Craig L.
Berger, Shelley L.
Allis, C. David
Document Type
Journal ArticlePublication Date
2005-04-13Keywords
Blotting, Western; Casein Kinase II; Chromatin Immunoprecipitation; *DNA Damage; DNA Repair; Histones; Nucleosomes; Phosphorylation; Saccharomyces cerevisiae; SerineLife Sciences
Medicine and Health Sciences
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Show full item recordAbstract
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.Source
Curr Biol. 2005 Apr 12;15(7):656-60. Link to article on publisher's siteDOI
10.1016/j.cub.2005.02.049Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33533PubMed ID
15823538Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.cub.2005.02.049