Polymerase chaperoning and multiple ATPase sites enable the E. coli DNA polymerase III holoenzyme to rapidly form initiation complexes.

@article{Downey2011PolymeraseCA,
  title={Polymerase chaperoning and multiple ATPase sites enable the E. coli DNA polymerase III holoenzyme to rapidly form initiation complexes.},
  author={Christopher D Downey and Elliott Crooke and Charles S McHenry},
  journal={Journal of molecular biology},
  year={2011},
  volume={412 3},
  pages={
          340-53
        }
}
Cellular replicases include three subassemblies: a DNA polymerase, a sliding clamp processivity factor, and a clamp loader complex. The Escherichia coli clamp loader is the DnaX complex (DnaX(3)δδ'χψ), where DnaX occurs either as τ or as the shorter γ that arises by translational frameshifting. Complexes composed of either form of DnaX are fully active clamp loaders, but τ confers important replicase functions including chaperoning the polymerase to the newly loaded clamp to form an initiation… CONTINUE READING

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Bacterial DNA Replicases

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