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文献和实验Drug Toxicity in E. coli Cells Expressing Human Topoisomerase I
for the major DNA-relaxing activity of the cell and is essential in an otherwise wild-type E. coli (3 ). E. coli and human topo I (htopoI) both catalyze the relaxation of negatively supercoiled DNA. However, they differ in the details of the reactions they catalyze
Plasmid DNA Supercoiling by DNA Gyrase
of two, and together with an ability to form and resolve DNA knots and catenanes, establishes gyrase as a type II topoisomerase.
Cleavage of Plasmid DNA by Eukaryotic Topoisomerase II
of the double helix. To maintain genomic integrity during the cleavage event, topoisomerase II forms covalent bonds between active site tyrosyl residues and the newly generated 5′-DNA termini. In addition to the critical cellular functions of the type II enzyme
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