8-oxodGTP incorporation by DNA polymerase beta is modified by active-site residue Asn279.

@article{Miller20008oxodGTPIB,
  title={8-oxodGTP incorporation by DNA polymerase beta is modified by active-site residue Asn279.},
  author={Holly Miller and Rajendra V V S Prasad and Samuel H. Wilson and Francis Johnson and Arthur P. Grollman},
  journal={Biochemistry},
  year={2000},
  volume={39 5},
  pages={1029-33}
}
To understand how the active site of a DNA polymerase might modulate the coding of 8-oxo-7,8-dihydrodeoxyguanine (8-oxodG), we performed steady-state kinetic analyses using wild-type DNA polymerase beta (pol beta) and two active-site mutants. We compared the coding of these polymerases by calculating the ratio of efficiencies for incorporation of dATP and dCTP opposite 8-oxodG and for incorporation of 8-oxodGTP opposite dA and dC. For wild-type pol beta, there is a 2:1 preference for… CONTINUE READING

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