H2AX prevents CtIP-mediated DNA end resection and aberrant repair in G1-phase lymphocytes

Beth A. Helmink, Anthony T. Tubbs, Yair Dorsett, Jeffrey J. Bednarski, Laura M. Walker, Zhihui Feng, Girdhar G. Sharma, Peter J. McKinnon, Junran Zhang, Craig H. Bassing and Barry P. Sleckman ()
Additional contact information
Beth A. Helmink: Washington University School of Medicine
Anthony T. Tubbs: Washington University School of Medicine
Yair Dorsett: Washington University School of Medicine
Jeffrey J. Bednarski: Washington University School of Medicine
Laura M. Walker: Washington University School of Medicine
Zhihui Feng: Washington University School of Medicine
Girdhar G. Sharma: Washington University School of Medicine
Peter J. McKinnon: St Jude Children’s Research Hospital
Junran Zhang: Washington University School of Medicine
Craig H. Bassing: Center for Childhood Cancer Research, Children’s Hospital of Philadelphia, University of Pennsylvania School of Medicine, Abramson Family Cancer Research Institute
Barry P. Sleckman: Washington University School of Medicine

Nature, 2011, vol. 469, issue 7329, 245-249

Abstract: Role for histone H2AX in maintaining genomic stability Antigen receptor loci contain numerous gene segments that are recombined in response to antigen stimulation. The RAG1/2 complex makes the double-strand breaks that initiate recombination. The ends of these breaks are hairpins that can only be cleaved by the Artemis nuclease. Barry Sleckman and colleagues show that the specificity for Artemis is dictated by the histone variant H2AX, in cooperation with the repair protein MDC1. In the absence of H2AX, another nuclease, CtIP, can open the ends but they are not joined efficiently by classical non-homogeneous end-joining, and this leads to genomic instability.

Date: 2011
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DOI: 10.1038/nature09585

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