A coproofreading Zn(2+)-dependent exonuclease within a bacterial replicase. Journal Article uri icon



  • The proofreading exonucleases of all DNA replicases contain acidic residues that chelate two Mg(2+) ions that participate in catalysis. DNA polymerase III holoenzymes contain their proofreading activity in a separate subunit, epsilon, which binds the polymerase subunit, alpha, through alpha's N-terminal php domain. Here we demonstrate that the alpha php domain contains a novel Zn(2+)-dependent 3' --> 5' exonuclease that preferentially removes mispaired nucleotides, providing the first example of a coediting nuclease.

publication date

  • May 1, 2006

has restriction

  • closed

Date in CU Experts

  • October 1, 2013 12:09 PM

Full Author List

  • Stano NM; Chen J; McHenry CS

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 1545-9993

Additional Document Info

start page

  • 458

end page

  • 459


  • 13


  • 5