Nucleic Acids Research Advance Access originally published online on January 20, 2009
Nucleic Acids Research 2009 37(3):712-720; doi:10.1093/nar/gkn1059
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Nucleic Acids Research, 2009, Vol. 37, No. 3 712-720
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Analysis of the eukaryotic topoisomerase II DNA gate: a single-molecule FRET and structural perspective
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
*To whom correspondence should be addressed. Tel: +1 919 684 6501; Fax: +1 919 684 8885; Email: hsieh{at}biochem.duke.edu
Received November 10, 2008. Revised December 15, 2008. Accepted December 17, 2008.
Type II DNA topoisomerases (topos) are essential and ubiquitous enzymes that perform important intracellular roles in chromosome condensation and segregation, and in regulating DNA supercoiling. Eukaryotic topo II, a type II topoisomerase, is a homodimeric enzyme that solves topological entanglement problems by using the energy from ATP hydrolysis to pass one segment of DNA through another by way of a reversible, enzyme-bridged double-stranded break. This DNA break is linked to the protein by a phosphodiester bond between the active site tyrosine of each subunit and backbone phosphate of DNA. The opening and closing of the DNA gate, a critical step for strand passage during the catalytic cycle, is coupled to this enzymatic cleavage/religation of the backbone. This reversible DNA cleavage reaction is the target of a number of anticancer drugs, which can elicit DNA damage by affecting the cleavage/religation equilibrium. Because of its clinical importance, many studies have sought to determine the manner in which topo II interacts with DNA. Here we highlight recent single-molecule fluorescence resonance energy transfer and crystallographic studies that have provided new insight into the dynamics and structure of the topo II DNA gate.
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