PMID:8383523
| Citation |
Ali, JA, Jackson, AP, Howells, AJ and Maxwell, A (1993) The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry 32:2717-24 |
|---|---|
| Abstract |
We have cloned and overexpressed a gene encoding a 43-kDa protein corresponding to the N-terminal fragment of the DNA gyrase B subunit. We show that this protein hydrolyzes ATP and binds coumarin drugs. The hydrolysis of ATP shows distinctly non-Michaelis-Menten kinetics and is consistent with a scheme in which the active form of the protein is a dimer, a conclusion supported by molecular weight studies. The coumarin drugs bind very tightly to the 43-kDa fragment, with novobiocin binding to the protein monomer and coumermycin A1 apparently inducing the formation of a dimer. The implications of these results with respect to the mechanism of supercoiling by DNA gyrase and the inhibition of gyrase by coumarin drugs are discussed. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Cloning, Molecular; Coumarins/metabolism; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/isolation & purification; DNA Topoisomerases, Type II/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Mathematics; Models, Theoretical; Molecular Weight; Peptide Fragments/isolation & purification; Peptide Fragments/metabolism; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism |
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