Ku is a 5′-dRP/AP lyase that excises nucleotide damage near broken ends

Steven A. Roberts, Natasha Strande, Martin D. Burkhalter, Christina Strom, Jody M. Havener, Paul Hasty and Dale A. Ramsden ()
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Steven A. Roberts: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Natasha Strande: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Martin D. Burkhalter: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Christina Strom: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Jody M. Havener: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Paul Hasty: The University of Texas Health Science Center at San Antonio, 15355 Lambda Drive, San Antonio, Texas 78245, USA
Dale A. Ramsden: Lineberger Comprehensive Cancer Center, and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA

Nature, 2010, vol. 464, issue 7292, 1214-1217

Abstract: End-to-end DNA repair Most agents that generate breaks in DNA leave 'dirty ends' that cannot reunite without some intervening steps to restore the integrity of the nucleotides at the break. In this work, Roberts et al. show that the non-homologous end joining (NHEJ) repair pathway requires a 5′-dRP/AP lyase activity to remove abasic sites. Surprisingly, this activity is catalysed by Ku70, which, with its partner Ku86, had previously been thought only to recognize broken DNA ends and to recruit other NHEJ proteins to that site.

Date: 2010
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DOI: 10.1038/nature08926

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