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- W1985896991 abstract "The replicative helicase of E. coli, DnaB, is a ring-shaped hexameric motor protein capable of unwinding double-stranded DNA (dsDNA) at a fork. It is thought to do this through “steric occlusion,” in which DnaB encircles and translocates along one single strand of DNA (ssDNA), forcing the other single strand (the occluded strand) to pass outside the ring. Using magnetic tweezers, we have performed single-molecule measurements of the unwinding activity of DnaB in which the dsDNA is destabilized by force applied to either the occluded or encircled strand. Based on measurements of the velocity of the motor as a function of force applied to the occluded strand, we conclude that DnaB does not unwind dsDNA with a “passive” mechanism, i.e. it does not simply rely on thermal fluctuations to open proximal basepairs before stepping. We also present preliminary data of DnaB activity with force applied to the encircled strand, which probes DnaB's possible mechanisms for binding and translocation along ssDNA. Finally, we will report on the effects of the helicase loader DnaC and the primase DnaG on DnaB activity." @default.
- W1985896991 created "2016-06-24" @default.
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- W1985896991 date "2009-02-01" @default.
- W1985896991 modified "2023-09-26" @default.
- W1985896991 title "Single-molecule Measurements Of DnaB" @default.
- W1985896991 doi "https://doi.org/10.1016/j.bpj.2008.12.2119" @default.
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