Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque

Marcelo Nöllmann, Michael D. Stone, Zev Bryant, Jeff Gore, Nancy J. Crisona, Seok Cheol Hong, Sylvain Mitelheiser, Anthony Maxwell, Carlos Bustamante, Nicholas R. Cozzarelli

Research output: Contribution to journalArticlepeer-review

86 Citations (Scopus)


E. coli DNA gyrase uses the energy of ATP hydrolysis to introduce essential negative supercoils into the genome, thereby working against the mechanical stresses that accumulate in supercoiled DNA. Using a magnetic-tweezers assay, we demonstrate that small changes in force and torque can switch gyrase among three distinct modes of activity. Under low mechanical stress, gyrase introduces negative supercoils by a mechanism that depends on DNA wrapping. Elevated tension or positive torque suppresses DNA wrapping, revealing a second mode of activity that resembles the activity of topoisomerase IV. This 'distal T-segment capture' mode results in active relaxation of left-handed braids and positive supercoils. A third mode is responsible for the ATP-independent relaxation of negative supercoils. We present a branched kinetic model that quantitatively accounts for all of our single-molecule results and agrees with existing biochemical data.

Original languageEnglish
Pages (from-to)264-271
Number of pages8
JournalNature Structural and Molecular Biology
Issue number4
Publication statusPublished - 2007 Apr

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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