نتایج جستجو برای: dna gyrase

تعداد نتایج: 507565  

Journal: :The Journal of biological chemistry 1999
E M Bahassi M H O'Dea N Allali J Messens M Gellert M Couturier

The F plasmid-carried bacterial toxin, the CcdB protein, is known to act on DNA gyrase in two different ways. CcdB poisons the gyrase-DNA complex, blocking the passage of polymerases and leading to double-strand breakage of the DNA. Alternatively, in cells that overexpress CcdB, the A subunit of DNA gyrase (GyrA) has been found as an inactive complex with CcdB. We have reconstituted the inactiv...

Journal: :The Biochemical journal 2013
Aurélie Bouige Amélie Darmon Jérémie Piton Mélanie Roue Stéphanie Petrella Estelle Capton Patrick Forterre Alexandra Aubry Claudine Mayer

In contrast with most bacteria which possess two type II topoisomerases (topoisomerase IV and DNA gyrase), Mycobacterium tuberculosis possesses only one, DNA gyrase, which is functionally a hybrid enzyme. Functional differences between the two type IIA topoisomerases are thought to be specified by a CTD (C-terminal DNA-binding domain), which controls DNA recognition. To explore the molecular me...

Journal: :Antimicrobial agents and chemotherapy 1996
I Morrissey K Hoshino K Sato A Yoshida I Hayakawa M G Bures L L Shen

Ofloxacin, a potent quinolone antibacterial agent, has a tricyclic ring structure with a methyl group attached to the asymmetric carbon at the C-3 position on the oxazine ring. The S isomer (DR-3355) of ofloxacin has antibacterial activity up to 2 orders of magnitude greater than that of the R isomer (DR-3354). This differential antibacterial activity was not due to different drug transport mec...

Journal: :Journal of bacteriology 2000
S W Knight B J Kimmel C H Eggers D S Samuels

The C-terminal domain of the A subunit of DNA gyrase, which we term Gac, is naturally synthesized in Borrelia burgdorferi as an abundant DNA-binding protein. Full-length GyrA, which includes the C-terminal domain, is also synthesized by the spirochete and functions as a subunit of DNA gyrase. We have disrupted synthesis of Gac as an independent protein and demonstrated that it is not essential ...

Journal: :Journal of Biological Chemistry 1997

Journal: :iranian journal of pharmacology and therapeutics 0
sattar ostadhadi brain and spinal cord injury research center, neuroscience institute tehran university of medical sciences, tehran, iran department of pharmacology, school of medicine, tehran university of medical sciences, tehran, iran mohsen rashidi samira zolfaghari jalal mardaneh vahid nikoui

appearance of bacteria resistant to antibacterial agents puts physicians in trouble and threatens the health of the world. the rapid development of bacterial resistance in escherichia coli to ciprofloxacin makes difficult the treatment of infectious diseases. so, detection of the locations of possible mutations in gyrase a gene ( gyra ) in these mutants is very important to determine the mechan...

Journal: :Journal of Bacteriology 1984

2000
Ian Morrissey John T. George

The quinolones inhibit the essential bacterial enzymes DNA gyrase and topoisomerase IV, which alter DNA topology after inserting a double-stranded break. DNA gyrase exists as an A2B2 tetramer, encoded by the gyrA and gyrB genes, and catalyses negative DNA supercoiling. Topoisomerase IV exists as a C2E2 tetramer encoded by the parC and parE genes, and is involved in chromosome partitioning. Prev...

Journal: :The Journal of antimicrobial chemotherapy 2006
Matthew J Ellington Neil Woodford

Sir, In their recent correspondence, Chu et al. noted the first observation of qnrA3 in salmonellae in Hong Kong, underlining the spread and diversity of plasmidic quinoloneresistance determinants worldwide. Such determinants now include qnrA1–5, qnrB and qnrS, some of which, at least, protect DNA gyrase, as well as the fluoroquinolone-acetylating variant of the aminoglycoside-modifying enzyme ...

Journal: :Antimicrobial agents and chemotherapy 2013
Sandra Aedo Yuk-Ching Tse-Dinh

Quinolones trap the covalent gyrase-DNA complex in Escherichia coli, leading to cell death. Processing activities for trapped covalent complex have not been characterized. A mutant strain lacking SbcCD nuclease activity was examined for both accumulation of gyrase-DNA complex and viability after quinolone treatment. Higher complex levels were found in ΔsbcCD cells than in wild-type cells after ...

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