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Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.

Dunderdale, H.J.; Benson, F.E.; Parsons, C.A.; Sharples, G.J.; Lloyd, R.G.; West, S.C.

Authors

H.J. Dunderdale

F.E. Benson

C.A. Parsons

R.G. Lloyd

S.C. West



Abstract

The recombination of DNA molecules has been reconstituted in vitro using 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.

Citation

Dunderdale, H., Benson, F., Parsons, C., Sharples, G., Lloyd, R., & West, S. (1991). Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins. Nature, 354(6354), 506-510

Journal Article Type Article
Publication Date 1991
Journal Nature
Print ISSN 0028-0836
Publisher Nature Research
Volume 354
Issue 6354
Pages 506-510
Publisher URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1758493




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