Abstract
Background: Human topoisomerase IIα unlinks catenated chromosomes and preferentially relaxes positive supercoils. Results: Supercoil chirality, twist density, and tension determine topoisomerase IIα relaxation rate and processivity. Conclusion: Strand passage rate is determined by the efficiency of transfer segment capture that is modulated by the topoisomerase C-terminal domains. Significance: Single-molecule measurements reveal the mechanism of chiral discrimination and tension dependence of supercoil relaxation by human topoisomerase IIα. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Seol, Y., Gentry, A. C., Osheroff, N., & Neuman, K. C. (2013). Chiral discrimination and writhe-dependent relaxation mechanism of human topoisomerase IIα. Journal of Biological Chemistry, 288(19), 13695–13703. https://doi.org/10.1074/jbc.M112.444745
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