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Nucleic Acids Research, 2003, Vol. 31, No. 17 4959-4964
© 2003 Oxford University Press

Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination

Niklas Schultz1, Elena Lopez2, Nasrollah Saleh-Gohari2 and Thomas Helleday*,1,2

1 Department of Genetic and Cellular Toxicology, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden and 2 The Institute for Cancer Studies, University of Sheffield, Medical School, Beech Hill Road, Sheffield S10 2RX, UK

*To whom correspondence should be addressed at The Institute for Cancer Studies, University of Sheffield, Medical School, Beech Hill Road, Sheffield S10 2RX, UK. Tel: +44 114 271 2993; Fax: +44 114 271 3515; Email: t.helleday{at}sheffield.ac.uk
Present address:
Elena Lopez, Department of Molecular and Cellular Biology, IMIM, 08003 Barcelona, Spain

Cells with non-functional poly(ADP-ribose) polymerase (PARP-1) show increased levels of sister chromatid exchange, suggesting a hyper recombination phenotype in these cells. To further investigate the involvement of PARP-1 in homologous recombination (HR) we investigated how PARP-1 affects nuclear HR sites (Rad51 foci) and HR repair of an endonuclease-induced DNA double-strand break (DSB). Several proteins involved in HR localise to Rad51 foci and HR-deficient cells fail to form Rad51 foci in response to DNA damage. Here, we show that PARP-1 mainly does not localise to Rad51 foci and that Rad51 foci form in PARP-1–/– cells, also in response to hydroxyurea. Furthermore, we show that homology directed repair following induction of a site-specific DSB is normal in PARP-1-inhibited cells. In contrast, inhibition or loss of PARP-1 increases spontaneous Rad51 foci formation, confirming a hyper recombination phenotype in these cells. Our data suggest that PARP-1 controls DNA damage recognised by HR and that it is not involved in executing HR as such.


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