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The Mechanism of Specific Cleavage of Supercoiled DNA by Human DNA Topoisomerase I: The Effect of Ligand Structure on the Catalytic Step of Cleavage
Eukaryotic DNA topoisomerase I (Topo) regulates the topological state of cell DNA and plays an important part in replication, transcription, repair, and recombination. Factors affecting the specific recognition of topologically stressed DNA were analyzed on the basis of the thermodynamic and kinetic...
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Published in: | Molecular biology (New York) 2003-03, Vol.37 (2), p.281-292 |
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container_title | Molecular biology (New York) |
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creator | Bugreev, D V Buneva, V N Nevinsky, G A |
description | Eukaryotic DNA topoisomerase I (Topo) regulates the topological state of cell DNA and plays an important part in replication, transcription, repair, and recombination. Factors affecting the specific recognition of topologically stressed DNA were analyzed on the basis of the thermodynamic and kinetic data on the Topo-DNA interaction and the X-ray data on human Topo. A model was advanced for possible structural changes occurring in the ligand after initial recognition. The effect of conformational changes in specific DNA on the catalytic step of the reaction was analyzed.[PUBLICATION ABSTRACT] |
doi_str_mv | 10.1023/A:1023306023933 |
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source | Springer Nature |
subjects | Data processing Deoxyribonucleic acid DNA DNA topoisomerase Ionizing radiation Kinetics Recombination Replication Thermodynamics Transcription |
title | The Mechanism of Specific Cleavage of Supercoiled DNA by Human DNA Topoisomerase I: The Effect of Ligand Structure on the Catalytic Step of Cleavage |
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