The interaction of four-way DNA junctions with resolving enzymes

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    Abstract

    Four-way DNA (Holliday) junctions are resolved into duplex species by the action of the junction-resolving enzymes, nucleases selective for the structure of helical branchpoints. These have been isolated from bacteria and their phages, archaea, yeasts and mammals, including humans. They are all dimeric proteins that bind with high selectivity to DNA junctions and generate bilateral cleavage within the lifetime of the DNA-protein complex. Recent success in obtaining X-ray crystal structures of resolving enzymes bound to DNA junctions has revealed how the structural selectivity of these enzymes is achieved.

    Original languageEnglish
    Pages (from-to)399-403
    Number of pages5
    JournalBiochemical Society Transactions
    Volume38
    DOIs
    Publication statusPublished - Apr 2010

    Keywords

    • DNA repair
    • genetic recombination
    • Holiday junction
    • molecular recognition
    • nuclease
    • T4 ENDONUCLEASE VII
    • HOLLIDAY-JUNCTION
    • GENETIC-RECOMBINATION
    • T7 ENDONUCLEASE
    • CRYSTAL-STRUCTURE
    • MAMMALIAN-CELLS
    • GENE-3 ENDONUCLEASE
    • YEAST
    • RESOLUTION
    • REPAIR

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