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Crystal structure of an octameric RuvA-Holliday junction complex

Roe, SM; Barlow, T; Brown, T; Oram, M; Keeley, A; Tsaneva, IR; Pearl, LH; (1998) Crystal structure of an octameric RuvA-Holliday junction complex. MOL CELL , 2 (3) 361 - 372.

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Abstract

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.

Type:Article
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

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