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Significance UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro. A MutL protein dimer can activate the monomeric UvrD helicase, but the mechanism of activation is not known. The 2B subdomain of UvrD is regulatory and is rotationally flexible. Here we show that binding of MutL to a UvrD–DNA substrate complex is accompanied by rotation of the 2B subdomain to form an active helicase. The results show the important role of the 2B subdomain in regulating helicase activity.

UvrD helicase activation by MutL involves rotation of its 2B subdomain