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Science 6 September 2002: Vol. 297. no. 5587, pp. 1686 - 1689 DOI: 10.1126/science.1074584
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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. Doherty1
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.
To whom correspondence should be addressed. E-mail:
AJD42{at}cam.ac.uk.
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