The RuvABC resolvasome.

@article{Dickman2002TheRR,
  title={The RuvABC resolvasome.},
  author={M. Dickman and S. M. Ingleston and S. Sedelnikova and J. Rafferty and R. G. Lloyd and J. Grasby and D. Hornby},
  journal={European journal of biochemistry},
  year={2002},
  volume={269 22},
  pages={
          5492-501
        }
}
  • M. Dickman, S. M. Ingleston, +4 authors D. Hornby
  • Published 2002
  • Biology, Medicine
  • European journal of biochemistry
  • 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… CONTINUE READING

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    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 37 REFERENCES
    Processing of recombination intermediates by the RuvABC proteins.
    426
    Formation of a RuvAB-Holliday junction complex in vitro.
    77
    Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
    128
    The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome
    24
    Structure of a multisubunit complex that promotes DNA branch migration
    169
    Structure and subunit composition of the RuvAB-Holliday junction complex.
    69