Nucleic Acids Research, 1993, Vol. 21, No. 8 1719-1725
© 1993
MOLECULAR BIOLOGY |
Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli
Department of Genetics, University of Nottingham, Queens Medical Centre Nottingham NG7 2UH, UK
Received February 19, 1993. Revised March 19, 1993. Accepted March 19, 1993.
The RuvAB, RuvC and RecG proteins of Escherlchla coil process intermediates In recombination and DNA repair Into mature products. RuvAB and RecG catalyse branch migration of Holliday junctions, while RuvC resolves these structures by nuclease cleavage around the point of strand exchange. The overlap between RuvAB and RecG was investigated using synthetic X-and Y-junctlons. RuvAB is a complex of RuvA and RuvB, with RuvA providing the DNA binding subunit and RuvB the ATPase activity that drives branch migration. Both RuvA and RecG form defined complexes with each of the junctions. The gel mobilities of these complexes suggests that the X-junctlon attracts two tetramers of RuvA, but mainly monomers of RecG. Dissociation of the junction In the presence of ATP requires high levels of RuvAB. RecG is shown to have a much higher specific activity to the extent that very little of this protein would be required to match RuvAB in vivo. Both proteins also dissociate a Y-junction, which Is consistent with helicase activity. However, RecG shows no ability to unwind more conventional substrates and the suggestion is made that its helicase activity is directed towards specific DNA structures such as junctions.
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