Nalidixic acid resistance: A second genetic character involved in DNA gyrase activity

DOI Web Site 被引用文献18件
  • Martin Gellert
    Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014
  • Kiyoshi Mizuuchi
    Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014
  • Mary H. O'Dea
    Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014
  • Tateo Itoh
    Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014
  • Jun-Ichi Tomizawa
    Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014

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<jats:p> ATP-dependent DNA supercoiling catalyzed by <jats:italic>Escherichia coli</jats:italic> DNA gyrase was inhibited by oxolinic acid, a compound similar to but more potent than nalidixic acid and a known inhibitor of DNA replication in <jats:italic>E. coli</jats:italic> . The supercoiling activity of DNA gyrase purified from nalidixic acid-resistant mutant ( <jats:italic>nalA</jats:italic> <jats:sup>R</jats:sup> ) bacteria was resistant to oxolinic acid. Thus, the <jats:italic>nalA</jats:italic> locus is responsible for a second component needed for DNA gyrase activity in addition to the component determined by the previously described locus for resistance to novobiocin and coumermycin ( <jats:italic>cou</jats:italic> ). Supercoiling of λ DNA in <jats:italic>E. coli</jats:italic> cells was likewise inhibited by oxolinic acid, but was resistant in the <jats:italic>nalA</jats:italic> <jats:sup>R</jats:sup> mutant. The inhibition by oxolinic acid of colicin E1 plasmid DNA synthesis in a cell-free system was largely relieved by adding resistant DNA gyrase. </jats:p> <jats:p>In the absence of ATP, DNA gyrase preparations relaxed supercoiled DNA; this activity was also inhibited by oxolinic acid, but not by novobiocin. It appears that the oxolinic acid-sensitive component of DNA gyrase is involved in the nicking-closing activity required in the supercoiling reaction. In the presence of oxolinic acid, DNA gyrase forms a complex with DNA, which can be activated by later treatment with sodium dodecyl sulfate and a protease to produce double-strand breaks in the DNA. This process has some similarities to the known properties of relaxation complexes.</jats:p>

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