Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone.

@article{Demott2002CovalentTO,
  title={Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone.},
  author={Michael S Demott and Ergin Beyret and Donny Wong and Brian Christopher Bales and Jae-Taeg Hwang and Marc M Greenberg and Bruce Demple},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 10},
  pages={
          7637-40
        }
}
Oxidized abasic residues in DNA constitute a major class of radiation and oxidative damage. Free radical attack on the nucleotidyl C-1' carbon yields 2-deoxyribonolactone (dL) as a significant lesion. Although dL residues are efficiently incised by the main human abasic endonuclease enzyme Ape1, we show here that subsequent excision by human DNA polymerase beta is impaired at dL compared with unmodified abasic sites. This inhibition is accompanied by accumulation of a protein-DNA cross-link not… CONTINUE READING
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