PMID:7991579
| Citation |
Howard, MT, Neece, SH, Matson, SW and Kreuzer, KN (1994) Disruption of a topoisomerase-DNA cleavage complex by a DNA helicase. Proc. Natl. Acad. Sci. U.S.A. 91:12031-5 |
|---|---|
| Abstract |
The type II DNA topoisomerases are targets for a variety of chemotherapeutic agents, including the antibacterial quinolones and several families of antitumor drugs. These agents stabilize an enzyme-DNA cleavage complex that consists of the topoisomerase covalently linked to the 5' phosphates of a double-stranded DNA break. Although the drug-stabilized cleavage complex is readily reversible, it can result in cell death by a mechanism that remains uncertain. Here we demonstrate that the action of a DNA helicase can convert the cleavage complex into a nonreversible DNA break by displacing DNA strands from the complex. Formation of a nonreversible DNA break, induced by a DNA helicase, could explain the cytotoxicity of these topoisomerase poisons. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Amsacrine; Bacteriophage T4/enzymology; Base Sequence; DNA Helicases; DNA Topoisomerases, Type II/isolation & purification; DNA Topoisomerases, Type II/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Models, Structural; Molecular Sequence Data; Plasmids/isolation & purification; Plasmids/metabolism; Protein Binding; Substrate Specificity |
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