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Formation and resolution of recombination intermediates by E. coliRecA and RuvC proteins

Nature volume 354, pages 506–510 (1991)Cite this article

Abstract

The recombination of DNA molecules has been reconstituted in vitrousing two purified enzymes from Escherichia coli. RecA protein catalyses homologous pairing and strand exchange reactions to form intermediate DNA structures that are acted upon by RuvC. The newly identified RuvC protein resolves the intermediates by specific endonucleolytic cleavage to produce recombinant DNA molecules.

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Author notes

  1. Gary J. Sharpies and Robert G. Lloyd: Genetics Department, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK

  2. Stephen C. West: To whom correspondence should be addressed.

Authors and Affiliations

  1. Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Herts, EN6 3LD, UK

    Hazel J. Dunderdale, Fiona E. Benson, Carol A. Parsons, Gary J. Sharpies, Robert G. Lloyd & Stephen C. West

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  1. Hazel J. Dunderdale
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  2. Fiona E. Benson
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  3. Carol A. Parsons
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  4. Gary J. Sharpies
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  5. Robert G. Lloyd
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  6. Stephen C. West
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Dunderdale, H., Benson, F., Parsons, C. et al. Formation and resolution of recombination intermediates by E. coliRecA and RuvC proteins. Nature 354, 506–510 (1991). https://doi.org/10.1038/354506a0

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