Abstract
The Escherichia coli UvrD protein is a 3′ to 5′ superfamily 1 DNA helicase that functions in nucleotide excision repair and methyl-directed mismatch repair of DNA, as well as DNA replication of certain plasmids. UvrD uses the energy of ATP binding and hydrolysis to unwind double-stranded DNA (dsDNA) and translocate along single-stranded DNA (ssDNA) with biased 3′ to 5′ directionality. Single turnover pre-steady state DNA unwinding kinetics experiments have shown that the UvrD dimer is the active form of the helicase in vitro, although a UvrD monomer can translocate along ssDNA with the same directionality as used in unwinding.
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