Threonine 79 is a hinge residue that governs the fidelity of DNA polymerase beta by helping to position the DNA within the active site.

@article{Maitra2002Threonine7I,
  title={Threonine 79 is a hinge residue that governs the fidelity of DNA polymerase beta by helping to position the DNA within the active site.},
  author={Mausumi Maitra and Andrew Gudzelak and Shu-xia Li and Yoshihiro Matsumoto and K. A. Eckert and Joachim Jager and Joann Balazs Sweasy},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 38},
  pages={
          35550-60
        }
}
DNA polymerase beta (pol beta) is an ideal system for studying the role of its different amino acid residues in the fidelity of DNA synthesis. In this study, the T79S variant of pol beta was identified using an in vivo genetic screen. T79S is located in the N-terminal 8-kDa domain of pol beta and has no contact with either the DNA template or the incoming dNTP substrate. The T79S protein produced 8-fold more multiple mutations in the herpes simplex virus type 1-thymidine kinase assay than wild… CONTINUE READING
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