We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Analysis of the eukaryotic topoisomerase II DNA gate: a single-molecule FRET and structural perspective.
- Authors
Collins, Tammy R L; Hammes, Gordon G; Hsieh, Tao-Shih
- Abstract
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.
- Publication
Nucleic acids research, 2009, Vol 37, Issue 3, p712
- ISSN
1362-4962
- Publication type
Journal Article
- DOI
10.1093/nar/gkn1059