Abstract
Replication Protein A (RPA) is the main eukaryotic single-stranded binding protein and is essential for most aspects of cellular DNA metabolism. RPA is able to unwind the dsDNA helix by binding to transiently forming single-stranded DNA bubbles [1]. We present single-molecule measurements of the dynamics of human RPA (hRPA) activity on dsDNA and ssDNA obtained with a magnetic tweezers-based assay. We show that hRPA-induced dsDNA-helix unwinding is strongly promoted by unwinding torque and can be reversed by rewinding torque exerted on the DNA.
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