Branch migration during homologous recombination: assembly of a RuvAB-Holliday junction complex in vitro

Kevin Hiom, Stephen C. West

    Research output: Contribution to journalArticle

    60 Citations (Scopus)

    Abstract

    The RuvA and RuvB proteins of E. coli promote the branch migration or movement of Holliday junctions during genetic recombination and DNA repair. Using small synthetic Holliday junctions in which the crossover point is confined near one end of the DNA molecule, we show that RuvAB-mediated branch migration occurs with a defined polarity. The assembly of RuvA and RuvB on the Holliday junction has been investigated by sedimentation analysis and by DNase I footprinting. We find that RuvA protein binds and protects all four strands of DNA at the crossover point, whereas RuvB protein binds the DNA asymmetrically. The polarity of branch migration is defined by the asymmetric assembly of the RuvAB branch migration complex relative to the junction and is consistent with a model in which RuvAB drives branch migration by passing the DNA through the hexameric rings of RuvB.

    Original languageEnglish
    Pages (from-to)787-793
    Number of pages7
    JournalCell
    Volume80
    Issue number5
    DOIs
    Publication statusPublished - 10 Mar 1995

      Fingerprint

    Keywords

    • Adenosine triphosphate
    • Bacterial proteins
    • Base sequence
    • DNA helicases
    • DNA repair
    • DNA, Bacterial
    • DNA-binding proteins
    • Escherichia coli
    • Escherichia coli proteins
    • Models, Genetic
    • Models, Molecular
    • Molecular sequence data
    • Recombination, Genetic

    Cite this