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

Bryan H. Schmidt, Alex B. Burgin, Joseph E. Deweese, Neil Osheroff and James M. Berger ()
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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
James M. Berger: University of California, Berkeley, California 94720, USA

Nature, 2010, vol. 465, issue 7298, 641-644

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.

Date: 2010
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DOI: 10.1038/nature08974

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