| Literature DB >> 26324265 |
Chunhui Chen1, Regis Villet2, George A Jacoby3, David C Hooper4.
Abstract
In order to study the interactions between Escherichia coli DNA gyrase and the gyrase interacting protein QnrB in vivo, we constructed a gyrB-gyrA fusion and validated its ability to correct the temperature-sensitive growth of gyrA and gyrB mutants. Like wild-type gyrA, the gyrB-gyrA fusion complemented a quinolone-resistant gyrA mutant to increase susceptibility. It functioned as an active type II topoisomerase, catalyzed negative supercoiling of DNA, was inhibited by quinolone, and was protected by QnrB.Entities:
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Year: 2015 PMID: 26324265 PMCID: PMC4604398 DOI: 10.1128/AAC.01845-15
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191