Abstract
DNA helicases are ATP-driven motor proteins that catalyse the separation of duplex DNA into its component single-strands. These are key intermediates in many cellular DNA transactions including replication, recombination and repair. In this study, we have investigated the kinetics of DNA translocation and unwinding by the AddAB helicase-nuclease; an enzyme which is involved in the initiation of double-stranded DNA break repair by homologous recombination. We show that AddAB displays extremely rapid and processive DNA unwinding activity powered by a single Superfamily 1A helicase domain.
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