The RuvABC resolvasome.

  title={The RuvABC resolvasome.},
  author={Mark J. Dickman and Stuart M. Ingleston and Svetlana E. Sedelnikova and John B. Rafferty and R. G. Lloyd and Jane A. Grasby and David P Hornby},
  journal={European journal of biochemistry},
  volume={269 22},
The RuvABC resolvasome of Escherichia coli catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. This process involves two key steps: branch migration, catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein, and resolution, which is catalysed by the RuvC endonuclease. We have quantified the interaction of the RuvA protein with synthetic Holliday junctions and have shown that the binding of… 

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Genetic and biochemical studies indicate that branch migration and resolution are coupled by direct interactions between the three proteins, possibly by the formation of a RuvABC complex.

Formation of a RuvAB-Holliday junction complex in vitro.

Results indicate that the formation of a (RuvAB-ATP)-Holliday junction complex represents the first step in the process of branch migration, and that branch migration is dependent upon ATP hydrolysis.

Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration.

Study of the specific interaction of the RuvA-RuvB complex with the Holliday structure using synthetic analogs prepared by annealing four oligonucleotides provides further evidence that theRuvA and RuvB complex recognizes the Hollidays junction and promotes branch migration in homologous recombination.

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Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli

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The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome

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