نتایج جستجو برای: dna gyrase

تعداد نتایج: 507565  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1981
L M Fisher K Mizuuchi M H O'Dea H Ohmori M Gellert

DNA gyrase, in the presence of the inhibitor oxolinic acid, can induce double-strand DNA breakage at specific sites. The sequences at several sites have been determined. In addition, the structure of complexes formed between DNA gyrase and restriction fragments containing an oxolinic acid-promoted cleavage site has been examined by DNase protection methods. DNA gyrase protects more than 120 bas...

2011
Xiaoli Xiong Elizabeth H. C. Bromley Peter Oelschlaeger Derek N. Woolfson James Spencer

Quinolones inhibit bacterial type II DNA topoisomerases (e.g. DNA gyrase) and are among the most important antibiotics in current use. However, their efficacy is now being threatened by various plasmid-mediated resistance determinants. Of these, the pentapeptide repeat-containing (PRP) Qnr proteins are believed to act as DNA mimics and are particularly prevalent in gram-negative bacteria. Predi...

2014
Manohary Rajendram Katherine A. Hurley Marie H. Foss Kelsey M. Thornton Jared T. Moore Jared T. Shaw Douglas B. Weibel

Antibiotics targeting DNA gyrase have been a clinical success story for the past half-century, and the emergence of bacterial resistance has fueled the search for new gyrase inhibitors. In this paper we demonstrate that a new class of gyrase inhibitors, the gyramides, are bacteriostatic agents that competitively inhibit the ATPase activity of Escherichia coli gyrase and produce supercoiled DNA ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1979
P O Brown C L Peebles N R Cozzarelli

We have identified a topoisomerase activity from Escherichia coli related to DNA gyrase (topoisomerase II): we designate it topoisomerase II'. It was constructed of two subunits, which were purified separately. One is the product of the gyrA (formerly nalA) gene and is identical to subunit A of DNA gyrase. The other is a 50,000-dalton protein, which we have purified to homogeneity and call v. v...

Journal: :Trends in microbiology 1997
A Maxwell

DNA gyrase is a remarkable enzyme, catalysing the seemingly complex reaction of DNA supercoiling. As gyrase is essential in prokaryotes, it is a good target for antibacterial agents. These agents have diverse chemical structures and interact with gyrase in a variety of ways.

Journal: :Current Biology 2006
Andrew D. Bates

A recent study has analysed the action of bacterial DNA gyrase on a single substrate DNA molecule, discriminating the initial DNA wrapping and subsequent supercoiling steps in the reaction cycle.

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2017
Pan F Chan Thomas Germe Benjamin D Bax Jianzhong Huang Reema K Thalji Eric Bacqué Anna Checchia Dongzhao Chen Haifeng Cui Xiao Ding Karen Ingraham Lynn McCloskey Kaushik Raha Velupillai Srikannathasan Anthony Maxwell Robert A Stavenger

A paucity of novel acting antibacterials is in development to treat the rising threat of antimicrobial resistance, particularly in Gram-negative hospital pathogens, which has led to renewed efforts in antibiotic drug discovery. Fluoroquinolones are broad-spectrum antibacterials that target DNA gyrase by stabilizing DNA-cleavage complexes, but their clinical utility has been compromised by resis...

Journal: :Journal of bacteriology 2009
Audrey Mérens Stéphanie Matrat Alexandra Aubry Christine Lascols Vincent Jarlier Claude-James Soussy Jean-Didier Cavallo Emmanuelle Cambau

MfpA(Mt) and QnrB4 are two newly characterized pentapeptide repeat proteins (PRPs) that interact with DNA gyrase. The mfpA(Mt) gene is chromosome borne in Mycobacterium tuberculosis, while qnrB4 is plasmid borne in enterobacteria. We expressed and purified the two PRPs and compared their effects on DNA gyrase, taking into account host specificity, i.e., the effect of MfpA(Mt) on M. tuberculosis...

2008
Sugopa Sengupta Valakunja Nagaraja

We assign a function for a small protein, YacG encoded by Escherichia coli genome. The NMR structure of YacG shows the presence of an unusual zinc-finger motif. YacG was predicted to be a part of DNA gyrase interactome based on protein-protein interaction network. We demonstrate that YacG inhibits all the catalytic activities of DNA gyrase by preventing its DNA binding. Topoisomerase I and IV a...

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