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- W2043323114 abstract "DNA topoisomerase regulates the topological state of DNA, which is very important for replication, transcription and recombination. The relaxation of negatively supercoiled DNA is catalyzed by bacterial DNA topoisomerase I (topoI) and this reaction requires Mg2+. We quantitatively studied the molecular interactions between Escherichia coli topoisomerase I (EctopoI) and pBAD/Thio supercoiled plasmid DNA using surface plasmon resonance (SPR) technique. The equilibrium dissociation constant (Kd) for EctopoI-pBAD/Thio interactions is determined to be about 8 nM. A slightly higher Kd value (∼15 nM) was obtained for Mg2+ coordinated EctopoI (Mg2+EctopoI)-pBAD/Thio interactions. In addition, we observed a larger dissociation rate constant (kd) for Mg2+EctopoI-pBAD/Thio interactions (∼0.043 s−1), compared to EctopoI-pBAD/Thio interactions (∼0.017 s−1). These results suggest that enzyme turnover during plasmid DNA relaxation is enhanced due to the presence of Mg2+." @default.
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- W2043323114 date "2015-01-01" @default.
- W2043323114 modified "2023-10-07" @default.
- W2043323114 title "Molecular Interaction between Escherichia Coli Topoisomerase I and pBAD/Thio Supercoiled Plasmid DNA" @default.
- W2043323114 doi "https://doi.org/10.1016/j.bpj.2014.11.2181" @default.
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