The RuvABC resolvasome.

@article{Dickman2002TheRR,
  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},
  year={2002},
  volume={269 22},
  pages={
          5492-501
        }
}
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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41 Citations
Background Citations
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Methods Citations
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41 Citations

The Role of RuvA Octamerization for RuvAB Function in Vitro and in Vivo*
TLDR
Results indicate strongly that RuvA octamerization is essential for the full biological activity of RuvABC.
Single-molecule study of RuvAB-mediated Holliday-junction migration.
TLDR
It is directly demonstrated that RuvAB is a highly processive DNA motor protein that is able to drive continuous and unidirectional branch migration of Holliday junctions at a well defined average speed over several kilobases through homologous sequences.
Electron microscopic single particle analysis of a tetrameric RuvA/RuvB/Holliday junction DNA complex.
Structure and Metal Binding Properties of a Poxvirus Resolvase*
TLDR
The crystal structure of the canarypox virus (CPV) resolvase is determined and a model of the CPV resolVase·Holliday junction complex provides insights into the consequences of these differences, including a plausible explanation for the weak sequence specificity exhibited by the poxvirus enzymes.
Caution! DNA Crossing: Crystal Structures of Holliday Junctions*
TLDR
The structures of DNA-only junctions and their geometries, as defined by sequence and ion-dependent interactions, are focused on.
Dissection of the functional domains of an archaeal Holliday junction helicase.
Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability.
Formation of a Stable RuvA Protein Double Tetramer Is Required for Efficient Branch Migration in Vitro and for Replication Fork Reversal in Vivo*
TLDR
It is shown that the need for RuvA tetramer-tetramer interactions for full RuvAB activity in vitro causes specifically an RFR defect in vivo, and this work demonstrates thatRuvA2KaP is a separation-of-function mutant, capable of homologous recombination but impaired for RFR.
Three-dimensional structural views of branch migration and resolution in DNA homologous recombination.
Holliday junction resolution
TLDR
Two main types of endonuclease, the HJ resolvases and the Mus81 nucleases, which process HJs and/or related intermediates (e.g. forks, D-loops and nicked HJs) are described.
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