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GyrBA融合蛋白的功能及其与QnrB和喹诺酮类药物的相互作用。

Functions of a GyrBA fusion protein and its interaction with QnrB and quinolones.

作者信息

Chen Chunhui, Villet Regis, Jacoby George A, Hooper David C

机构信息

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.

Division of Infectious Diseases, Massachusetts General Hospital, Boston, Massachusetts, USA.

出版信息

Antimicrob Agents Chemother. 2015 Nov;59(11):7124-7. doi: 10.1128/AAC.01845-15. Epub 2015 Aug 31.

DOI:10.1128/AAC.01845-15
PMID:26324265
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4604398/
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.

摘要

为了在体内研究大肠杆菌DNA促旋酶与促旋酶相互作用蛋白QnrB之间的相互作用，我们构建了gyrB-gyrA融合体，并验证了其校正gyrA和gyrB突变体温度敏感生长的能力。与野生型gyrA一样，gyrB-gyrA融合体互补喹诺酮抗性gyrA突变体以增加敏感性。它作为一种活性II型拓扑异构酶发挥作用，催化DNA的负超螺旋，被喹诺酮抑制，并受到QnrB的保护。

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