Author:
Chen Chunhui,Villet Regis,Jacoby George A.,Hooper David C.
Abstract
ABSTRACTIn order to study the interactions betweenEscherichia coliDNA gyrase and the gyrase interacting protein QnrBin vivo, we constructed agyrB-gyrAfusion and validated its ability to correct the temperature-sensitive growth ofgyrAandgyrBmutants. Like wild-typegyrA, thegyrB-gyrAfusion complemented a quinolone-resistantgyrAmutant 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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
2 articles.
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