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The DNA glycosylase AlkD uses a non-base-flipping mechanism to excise bulky lesions

Author

Listed:
  • Elwood A. Mullins

    (Vanderbilt University)

  • Rongxin Shi

    (Vanderbilt University)

  • Zachary D. Parsons

    (Vanderbilt University)

  • Philip K. Yuen

    (University of California, Davis)

  • Sheila S. David

    (University of California, Davis)

  • Yasuhiro Igarashi

    (Biotechnology Research Center, Toyama Prefectural University)

  • Brandt F. Eichman

    (Vanderbilt University)

Abstract

Crystal structures of the DNA glycosylase AlkD with DNA containing various modified bases show that neither substrate recognition nor catalysis use a base-flipping mechanism; instead, AlkD scans the phosphodeoxyribose backbone for increased cationic charge imparted by the alkylated base, and then uses the positive charge to facilitate cleavage of the glycosidic bond, thus explaining the specificity of AlkD for cationic lesions.

Suggested Citation

  • Elwood A. Mullins & Rongxin Shi & Zachary D. Parsons & Philip K. Yuen & Sheila S. David & Yasuhiro Igarashi & Brandt F. Eichman, 2015. "The DNA glycosylase AlkD uses a non-base-flipping mechanism to excise bulky lesions," Nature, Nature, vol. 527(7577), pages 254-258, November.
    • Handle: RePEc:nat:nature:v:527:y:2015:i:7577:d:10.1038_nature15728
    DOI: 10.1038/nature15728
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    Cited by:

    1. Elwood A. Mullins & Jonathan Dorival & Gong-Li Tang & Dale L. Boger & Brandt F. Eichman, 2021. "Structural evolution of a DNA repair self-resistance mechanism targeting genotoxic secondary metabolites," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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