Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.

@article{Li2000IntactMA,
  title={Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.},
  author={Xin Li and A. Lili Lu},
  journal={Nucleic acids research},
  year={2000},
  volume={28 23},
  pages={
          4593-603
        }
}
Escherichia coli MutY is an adenine and a weak guanine DNA glycosylase active on DNA substrates containing A/G, A/8-oxoG, A/C or G/8-oxoG mismatches. A truncated form of MutY (M25, residues 1-226) retains catalytic activity; however, the C-terminal domain of MutY is required for specific binding to the 8-oxoG and is critical for mutation avoidance of oxidative damage. Using alkylation interference experiments, the determinants of the truncated and intact MutY were compared on A/8-oxoG… CONTINUE READING

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