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.
RuvABC Is Required to Resolve Holliday Junctions That Accumulate following Replication on Damaged Templates in Escherichia coli*
TLDR
Results indicate that the Holliday junctions observed in ruv mutants are intermediates of a repair pathway that is distinct from that of the recovery of arrested replication forks and a model is proposed in which RuvABC is required to resolve junctions that arise during the repair of a subset of nonarresting lesions after replication has passed through the template.
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.
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References

SHOWING 1-10 OF 37 REFERENCES
Processing of recombination intermediates by the RuvABC proteins.
  • S. West
  • Biology
    Annual review of genetics
  • 1997
TLDR
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.
TLDR
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.
TLDR
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.
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
TLDR
It is suggested that the RuvA and RuvB proteins play a specific role in the branch migration of Holliday junctions during postreplication repair of DNA damage in E. coli.
Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli
TLDR
The observed synergy between RuvB and RuvC provides new insight into the structure and function of a RuvABC complex that is capable of facilitating branch migration and resolution of Holliday junctions via a concerted enzymatic mechanism.
The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome
TLDR
It is shown that two negative charges on each subunit of the pin are crucial and facilitate junction targeting by preventing binding to duplex DNA and also constrain branch migration by RuvAB in a manner critical for junction processing.
Structure of a multisubunit complex that promotes DNA branch migration
TLDR
A molecular model for branch migration is proposed, a unique feature of which is the role played by the two oppositely oriented RuvB ring motors.
Structure and subunit composition of the RuvAB-Holliday junction complex.
The E. coli RuvA and RuvB proteins, which are involved in the late stages of recombination and the recombinational repair of damaged DNA, bind to Holliday junctions and promote branch migration. We…
Interactions between RuvA and RuvC at Holliday junctions: inhibition of junction cleavage and formation of a RuvA-RuvC-DNA complex.
TLDR
It is shown that RuvA inhibits junction cleavage by RuvC, probably by sandwiching the junction between two tetramers, and suggested that recognition of the target may provide a trigger for dissociatingRuvA, allowing the junction to be folded and cleaved byRuvC.
Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.
TLDR
The solved crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1-A resolution revealed an open concave architecture with a four-fold symmetry, which suggests a possible scheme for successive base pair rearrangements, which may account for smooth Holliday Junction movement without segmental unwinding.
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