Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme.

@article{Wieczorek2010OnlyOA,
  title={Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme.},
  author={Anna Wieczorek and Christopher D Downey and H. Garry Dallmann and Charles S McHenry},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 38},
  pages={
          29049-53
        }
}
The DnaX complex (DnaX(3)δδ'χ psi) within the Escherichia coli DNA polymerase III holoenzyme serves to load the dimeric sliding clamp processivity factor, β(2), onto DNA. The complex contains three DnaX subunits, which occur in two forms: τ and the shorter γ, produced by translational frameshifting. Ten forms of E. coli DnaX complex containing all possible combinations of wild-type or a Walker A motif K51E variant τ or γ have been reconstituted and rigorously purified. DnaX complexes containing… CONTINUE READING

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