Functions of a GyrBA fusion protein and its interaction with QnrB and quinolones.
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.
Division of Infectious Diseases, Massachusetts General Hospital, Boston, Massachusetts, USA Institute of Antibiotics, Huashan Hospital, Fudan University, and Key Laboratory of Clinical Pharmacology of Antibiotics, National Health and Family Planning Commission, Shanghai, China.
Chunhui
C
Chen
Division of Infectious Diseases, Massachusetts General Hospital, Boston, Massachusetts, USA.
Regis
R
Villet
Lahey Hospital and Medical Center, Burlington, Massachusetts, USA.
George A
GA
Jacoby
Division of Infectious Diseases, Massachusetts General Hospital, Boston, Massachusetts, USA dhooper@mgh.harvard.edu.
David C
DC
Hooper
D000890:Anti-Infective Agents / Q000378:metabolism / Q000494:pharmacology; D027081:DNA Gyrase / Q000235:genetics / Q000378:metabolism*; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015363:Quinolones / Q000378:metabolism* / Q000494:pharmacology*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*
D000890:Anti-Infective Agents; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D015363:Quinolones; D011993:Recombinant Fusion Proteins; D027081:DNA Gyrase