Abstract
Resolution of four-way Holliday junctions (HJs) is a critical intermediate step of Homologous Recombination. HJs are processed by abundant junction-resolving endonucleases that introduce two hydrolytic cleavages. Although their catalytic activity and interaction mode with HJ-DNA have been characterized in great detail by biochemical and structural studies, it remains unclear how the endonucleases find their substrate located in kilobase pairs of duplex DNA. Here, we studied the interaction of the T7 endonuclease I with a long dsDNA molecule that has a junction located at its center.
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