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Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA

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Listed:
  • Cai-Guang Yang

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Chengqi Yi

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Erica M. Duguid

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Christopher T. Sullivan

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Xing Jian

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Phoebe A. Rice

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Chuan He

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

Abstract

Escherichia coli AlkB and its human homologues ABH2 and ABH3 repair DNA/RNA base lesions by using a direct oxidative dealkylation mechanism. ABH2 has the primary role of guarding mammalian genomes against 1-meA damage by repairing this lesion in double-stranded DNA (dsDNA), whereas AlkB and ABH3 preferentially repair single-stranded DNA (ssDNA) lesions and can repair damaged bases in RNA. Here we show the first crystal structures of AlkB–dsDNA and ABH2–dsDNA complexes, stabilized by a chemical cross-linking strategy. This study reveals that AlkB uses an unprecedented base-flipping mechanism to access the damaged base: it squeezes together the two bases flanking the flipped-out one to maintain the base stack, explaining the preference of AlkB for repairing ssDNA lesions over dsDNA ones. In addition, the first crystal structure of ABH2, presented here, provides a structural basis for designing inhibitors of this human DNA repair protein.

Suggested Citation

  • Cai-Guang Yang & Chengqi Yi & Erica M. Duguid & Christopher T. Sullivan & Xing Jian & Phoebe A. Rice & Chuan He, 2008. "Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA," Nature, Nature, vol. 452(7190), pages 961-965, April.
    • Handle: RePEc:nat:nature:v:452:y:2008:i:7190:d:10.1038_nature06889
    DOI: 10.1038/nature06889
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