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Research Article

Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins.

P Hallett, A Maxwell
P Hallett
Department of Biochemistry, University of Leicester, United Kingdom.
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A Maxwell
Department of Biochemistry, University of Leicester, United Kingdom.
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DOI: 10.1128/AAC.35.2.335
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ABSTRACT

Using the techniques of gap misrepair mutagenesis and site-directed mutagenesis, we have generated two novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein. DNA sequencing showed these mutations to be Ser-83----Ala and Gln-106----Arg. The mutant proteins were overproduced and purified, and their enzymatic properties were analyzed and compared with those of the wild-type enzyme. With ciprofloxacin and other quinolones, the inhibition of DNA supercoiling, relaxation, and decatenation and the induction of DNA cleavage were investigated for both wild-type and mutant enzymes. In each assay, the mutant enzymes were found to require approximately 10 times more drug to inhibit the reaction or induce cleavage than was the wild-type enzyme. However, the Ca2(+)-directed DNA cleavage reaction was indistinguishable for wild-type and mutant gyrases. We discuss models for the gyrase-mediated bactericidal effects of quinolone drugs.

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Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins.
P Hallett, A Maxwell
Antimicrobial Agents and Chemotherapy Feb 1991, 35 (2) 335-340; DOI: 10.1128/AAC.35.2.335

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Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins.
P Hallett, A Maxwell
Antimicrobial Agents and Chemotherapy Feb 1991, 35 (2) 335-340; DOI: 10.1128/AAC.35.2.335
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