Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy.

@article{DeRose2003ElucidationOT,
  title={Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy.},
  author={Eugene F. DeRose and Thomas Reed Darden and Scott B Harvey and Scott Thomas Gabel and F. W. Perrino and Roel M. Schaaper and Robert E. London},
  journal={Biochemistry},
  year={2003},
  volume={42 13},
  pages={
          3635-44
        }
}
The DNA polymerase III holoenzyme (HE) is the primary replicative polymerase of Escherichia coli. The epsilon (epsilon) subunit of HE provides the 3'-->5' exonucleolytic proofreading activity for this complex. Epsilon consists of two domains: an N-terminal domain containing the proofreading exonuclease activity (residues 1-186) and a C-terminal domain required for binding to the polymerase (alpha) subunit (residues 187-243). In addition to alpha, epsilon also binds the small (8 kDa) theta… CONTINUE READING
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