Abstract
DNA Mismatch Repair (MMR) is a conserved system that maintains genomic fidelity through correction of DNA replication errors. However, DNA MMR displays mutagenic actions that contribute to DNA triplet repeat expansions. Here we used single molecule FRET measurements to characterize MMR protein binding to DNA structures containing triplet repeats. DNA primary and secondary structures were demonstrated to affect strand slippage dynamics as well as DNA-protein binding kinetics in trinucleotide repeat DNA hairpins and related three-way junctions.
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