Separation-of-function mutants unravel the dual-reaction mode of human 8-oxoguanine DNA glycosylase.

  title={Separation-of-function mutants unravel the dual-reaction mode of human 8-oxoguanine DNA glycosylase.},
  author={Bj\orn Dalhus and Monika Forsbring and Ina H\oydal Helle and Erik Sebastian Vik and Rune Johansen Forstr\om and Paul Hoff Backe and Ingrun Alseth and Magnar Bj\or{\aa}s},
  volume={19 1},
7,8-Dihydro-8-oxoguanine (8oxoG) is a major mutagenic base lesion formed when reactive oxygen species react with guanine in DNA. The human 8oxoG DNA glycosylase (hOgg1) recognizes and initiates repair of 8oxoG. hOgg1 is acknowledged as a bifunctional DNA glycosylase catalyzing removal of the damaged base followed by cleavage of the backbone of the intermediate abasic DNA (AP lyase/β-elimination). When acting on 8oxoG-containing DNA, these two steps in the hOgg1 catalysis are considered coupled… CONTINUE READING

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