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A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases

Author

Listed:
  • Bryan H. Schmidt

    (University of California, Berkeley, California 94720, USA)

  • Alex B. Burgin

    (Emerald BioStructures, Bainbridge Island, Washington 98110, USA)

  • Joseph E. Deweese

    (Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA)

  • Neil Osheroff

    (Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA
    Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA)

  • James M. Berger

    (University of California, Berkeley, California 94720, USA)

Abstract

A unified mechanism for topoisomerases Topoisomerases transiently make either single-strand (type I topoisomerases) or double-strand (type II) breaks in DNA to prevent the build-up of topological stress and tangles as the genome is transcribed, replicated or repaired. Type II topoisomerases had been postulated to use a two-metal mechanism to break the duplex DNA. Here, Schmidt et al. have solved the structure of a yeast type II enzyme and find that a new variation of the classical mechanism is used, and that this mechanism can also perform the type of cleavage that is normally the province of type I topoisomerases.

Suggested Citation

  • Bryan H. Schmidt & Alex B. Burgin & Joseph E. Deweese & Neil Osheroff & James M. Berger, 2010. "A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases," Nature, Nature, vol. 465(7298), pages 641-644, June.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7298:d:10.1038_nature08974
    DOI: 10.1038/nature08974
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