Abstract
RecA protein is an essential component directly involved in general genetic recombination in Escherichia coli1,2. In the presence of ATP, RecA protein promotes in vitro pairing of homologous DNA molecules3–9, unidirectional elongation of heteroduplex joints7,10,12 and concerted reciprocal strand exchange13,14. These activities of the protein can explain some important steps in genetic recombination (see ref. 15 for review). When negative-superhelical closed-circular double-stranded DNA (form I DNA) is a substrate, RecA protein catalyses a cycle of sequential reactions: formation and dissociation of D-loops, and inactivation and reactivation of the duplex as a substrate for D-loop formation16,55. We now present evidence that, in the presence of ATP, RecA protein unwinds the double helix of form I DNA to produce positive-superhelical turns which can be relaxed by eukaryotic topoisomerase I and that, by this process, closed-circular double-stranded DNA with an extraordinarily large number of negative-superhelical turns can be formed in physiological conditions. This ATP-dependent unwinding of the double-helix might promote dissociation of D-loops in form I DNA, followed by inactivation of the form I DNA and the elongation of heteroduplex joints, as suggested by our previous studies16,17,55.
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Ohtani, T., Shibata, T., Iwabuchi, Ma. et al. ATP-dependent unwinding of double helix in closed circular DNA by RecA protein of E. coli. Nature 299, 86–89 (1982). https://doi.org/10.1038/299086a0
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DOI: https://doi.org/10.1038/299086a0
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