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  • Title: Quinolone-resistant mutations of DNA gyrase increase sensitivity to acriflavine.
    Author: Funatsuki K, Tanaka R, Inagaki S, Konno H, Katoh K, Nakamura H.
    Journal: Biol Pharm Bull; 1998 Jul; 21(7):667-72. PubMed ID: 9703246.
    Abstract:
    DNA gyrases were constructed to possess the quinolone-resistant (D87N in GyrA or K447E in GyrB) and acrB (S759R-R760C in GyrB) mutations and their sensitivities to acriflavine and oxolinic acid were examined. Both quinolone-resistant mutations in GyrA and GyrB increased acriflavine sensitivities in the supercoiling assay irrespective of the co-presence of the acrB mutation. In the DNA binding assay, however, the hypersensitvity caused by the GyrB (K447E) mutation was observed only in the co-presence of the acrB mutation; the presence of the acrB mutation, which not affecting acriflavine sensitivity, reduces the extent of DNA binding, as reported previously. Thus, the quinolone-resistant mutation site in GyrB is likely to be involved in DNA binding which is not detectable in acrB+ gyrase. Furthermore, oxolinic acid was found to enhance DNA binding of the gyrase having GyrB (acrB-K447E), supporting a recent proposal that quinolone binding to the DNA-gyrase complex does not require DNA breakage.
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