西亚试剂：HP1- mobilization promotes chromatin changes that initiate

发布时间：2025-06-27

Nature 453, 682-686 (29 May 2008) | doi:10.1038/nature06875; Received 14 November 2007; Accepted 28 February 2008; Published online 27 April 2008

 

HP1- mobilization promotes chromatin changes that initiate the DNA damage response

Nabieh Ayoub1, Anand D. Jeyasekharan1, Juan A. Bernal1 & Ashok R. Venkitaraman1

Correspondence to: Ashok R. Venkitaraman1 Correspondence and requests for materials should be addressed to A.R.V. (Email: arv22@cam.ac.uk).

Minutes after DNA damage, the variant histone H2AX is phosphorylated by protein kinases of the phosphoinositide kinase family, including ATM, ATR or DNA-PK1. Phosphorylated ()-H2AX—which recruits molecules that sense or signal the presence of DNA breaks, activating the response that leads to repair2, 3—is the earliest known marker of chromosomal DNA breakage. Here we identify a dynamic change in chromatin that promotes H2AX phosphorylation in mammalian cells. DNA breaks swiftly mobilize heterochromatin protein 1 (HP1)- (also called CBX1), a chromatin factor bound to histone H3 methylated on lysine 9 (H3K9me). Local changes in histone-tail modifications are not apparent. Instead, phosphorylation of HP1- on amino acid Thr 51 accompanies mobilization, releasing HP1- from chromatin by disrupting hydrogen bonds that fold its chromodomain around H3K9me. Inhibition of casein kinase 2 (CK2), an enzyme implicated in DNA damage sensing and repair4, 5, 6, suppresses Thr 51 phosphorylation and HP1- mobilization in living cells. CK2 inhibition, or a constitutively chromatin-bound HP1- mutant, diminishes H2AX phosphorylation. Our findings reveal an unrecognized signalling cascade that helps to initiate the DNA damage response, altering chromatin by modifying a histone-code mediator protein, HP1, but not the code itself.

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