Formation and resolution of recombination intermediates by E. coliRecA and RuvC proteins
- 1 December 1991
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 354 (6354), 506-510
- https://doi.org/10.1038/354506a0
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.Keywords
This publication has 33 references indexed in Scilit:
- Stable three-stranded DNA made by RecA protein.Proceedings of the National Academy of Sciences of the United States of America, 1991
- Pairing of homologous DNA sequences by proteins: evidence for three-stranded DNA.Genes & Development, 1990
- RecA protein reinitiates strand exchange on isolated protein-free DNA intermediates: An ADP-resistant processJournal of Molecular Biology, 1990
- Homologous pairing and the formation of nascent synaptic intermediates between regions of duplex DNA by RecA proteinCell, 1989
- Duplex-duplex interactions catalyzed by recA protein allow strand exchanges to pass double-strand breaks in DNACell, 1984
- Role of RecA protein spiral filaments in genetic recombinationNature, 1984
- Enzymatic formation of biparental figure-eight molecules from plasmid DNA and their resolution in E. coliCell, 1983
- T4 endonuclease VII cleaves holliday structuresCell, 1982
- Concerted strand exchange and formation of Holliday structures by E. coli RecA proteinCell, 1981
- A mechanism for gene conversion in fungiGenetics Research, 1964