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Science 6 September 2002:
Vol. 297. no. 5587, pp. 1686 - 1689
DOI: 10.1126/science.1074584

Reports

Identification of a DNA Nonhomologous End-Joining Complex in Bacteria

Geoffrey R. Weller,1* Boris Kysela,2* Rajat Roy,3* Louise M. Tonkin,1 Elizabeth Scanlan,4 Marina Della,1 Susanne Krogh Devine,4 Jonathan P. Day,5 Adam Wilkinson,5 Fabrizio d'Adda di Fagagna,3 Kevin M. Devine,4 Richard P. Bowater,5 Penny A. Jeggo,2 Stephen P. Jackson,3 Aidan J. Doherty1dagger

In eukaryotic cells, double-strand breaks (DSBs) in DNA are generally repaired by the pathway of homologous recombination or by DNA nonhomologous end joining (NHEJ). Both pathways have been highly conserved throughout eukaryotic evolution, but no equivalent NHEJ system has been identified in prokaryotes. The NHEJ pathway requires a DNA end-binding component called Ku. We have identified bacterial Ku homologs and show that these proteins retain the biochemical characteristics of the eukaryotic Ku heterodimer. Furthermore, we show that bacterial Ku specifically recruits DNA ligase to DNA ends and stimulates DNA ligation. Loss of these proteins leads to hypersensitivity to ionizing radiation in Bacillus subtilis. These data provide evidence that many bacteria possess a DNA DSB repair apparatus that shares many features with the NHEJ system of eukarya and suggest that this DNA repair pathway arose before the prokaryotic and eukaryotic lineages diverged.

1 Cambridge Institute for Medical Research & Department of Haematology, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK.
2 Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.
3 Wellcome Trust/Cancer Research UK, Institute of Cancer and Developmental Biology and Department of Zoology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK.
4 Department of Genetics, Smurfit Institute, Trinity College Dublin, Dublin 2, Republic of Ireland.
5 School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: AJD42{at}cam.ac.uk.


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