DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism

@article{Roca1994DNATB,
  title={DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism},
  author={J. Roca and JAMES C. Wang},
  journal={Cell},
  year={1994},
  volume={77},
  pages={609-616}
}
DNA substrates in which a supercoiled DNA is singly linked to a nicked or relaxed DNA ring were used to analyze the transport of one DNA ring through another by yeast DNA topoisomerase II. The enzyme binds preferentially to the supercoiled DNA and promotes decatenation efficiently upon binding of a nonhydrolyzable ATP analog. Analysis of the reaction products shows that the nicked or relaxed DNA ring released is not associated with the enzyme-supercoiled DNA complex. These results favor a two… Expand
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Conversion of DNA gyrase into a conventional type II topoisomerase.
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Coupling between ATP Binding and DNA Cleavage by DNA Topoisomerase II
Topoisomerase II drives DNA transport by hydrolyzing one ATP.
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