1994
DOI: 10.1073/pnas.91.21.9901
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Dissociation of RecA filaments from duplex DNA by the RuvA and RuvB DNA repair proteins.

Abstract: The RuvA and RuvB proteins of Escherichia coUl act late in recombination and DNA repair to catalyze the branch migration of Holliday junctions made by RecA. In this paper, we show that addition of RuvAB to supercoiled DNA that is bound by RecA leads to the rapid dis tion of the *To whom reprint requests should be addressed. 9901The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solel… Show more

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Cited by 40 publications
(23 citation statements)
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“…Using these experimental conditions, we could follow the interaction between RecA and dsDNA in the region of synapsis almost exclusively. Only a very small proportion of covalently closed plasmid DNA molecules was covered with RecA resulting in the formation of extremely negatively supercoiled plasmid DNA, form X, after relaxation with topoisomerase I (Ohtani et al 1982;Adams et al 1994) (Fig. 6B).…”
Section: Discussionmentioning
confidence: 99%
“…Using these experimental conditions, we could follow the interaction between RecA and dsDNA in the region of synapsis almost exclusively. Only a very small proportion of covalently closed plasmid DNA molecules was covered with RecA resulting in the formation of extremely negatively supercoiled plasmid DNA, form X, after relaxation with topoisomerase I (Ohtani et al 1982;Adams et al 1994) (Fig. 6B).…”
Section: Discussionmentioning
confidence: 99%
“…The action of RecG following RecA-mediated DNA strand exchange and DNA repair could move the crossover backwards and ultimately reconstruct the framework of a replication fork without the action of RuvC or a similar Holliday junction resolvase (Kuzminov 1996b). The RuvA and RuvB proteins also displace RecA protein from DNA under some in vitro conditions, suggesting an additional function for these proteins in vivo (Adams et al 1994). However, the RecFOR proteins also appear to modulate RecA filament assembly and disassembly, and the fate of RecA filaments may turn out to be a more complex affair involving interactions with the RuvAB, RecFOR, and perhaps other proteins.…”
Section: Quantifying Step 1 Under Normal Growth Conditionsmentioning
confidence: 99%
“…RuvA and RuvB form a complex composed of one or two tetramers of RuvA and two hexamers of RuvB that catalyze branch migration of Holliday junctions (HJs) using the energy provided by ATP hydrolysis. The RuvAB helicase activity extends the heteroduplex DNA region and is thought to displace the RecA protein filament facilitating the loading of RuvC onto the HJ complex (30,31). Subsequently, the endonuclease activity of RuvC resolves the recombination intermediate by introducing nicks in two of the four DNA strands (29), producing nicked duplexes that can be sealed by a DNA ligase.…”
mentioning
confidence: 99%