Crystal structure of an octameric RuvA-Holliday junction complex.
361 - 372.
Holliday junctions occur as intermediates in homologous recombination and DNA repair. In bacteria, resolution of Holliday junctions is accomplished by the RuvABC system, consisting of a junction-specific helicase complex RuvAB, which promotes branch migration, and a junction-specific endonuclease RuvC, which nicks two strands. The crystal structure of a complex between the RuvA protein of M. leprae and a synthetic four-way junction has now been determined. Rather than binding on the open surface of a RuvA tetramer as previously suggested, the DNA is sandwiched between two RuvA tetramers, which form a closed octameric shell, stabilized by a conserved tetramer-tetramer interface. Interactions between the DNA backbone and helix-hairpin-helix motifs from both tetramers suggest a mechanism for strand separation promoted by RuvA.
|Title:||Crystal structure of an octameric RuvA-Holliday junction complex|
|Keywords:||ESCHERICHIA-COLI RUVA, DNA HELICASE ACTIVITY, BRANCH MIGRATION, GENETIC-RECOMBINATION, IN-VITRO, RECA PROTEIN, HOMOLOGOUS RECOMBINATION, MOLECULAR MECHANISMS, STRAND EXCHANGE, RESOLUTION|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology|
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