DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein.
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منابع مشابه
Purification and properties of DNA gyrase from Vibrio cholerae.
The DNA gyrase was purified from Vibrio cholerae strain 569B. It appeared to be composed of two subunits of Mr 120,000 and 97,000 and had a great deal of similarity to the Escherichia coli gyrase. Unlike the E. coli enzyme, however, it could neither relax supercoiled DNA nor induce a cleavage of double-stranded DNA, under experimental conditions in which E. coli gyrase could do so.
متن کاملDNA gyrase: affinity chromatography on novobiocin-Sepharose and catalytic properties.
Novobiocin-Sepharose was prepared by coupling of novobiocin to Epoxy-activated Sepharose 6B and used as an affinity adsorbent. Four novobiocin-binding proteins were isolated from crude extracts of Escherichia coli with molecular weights of 105, 92, 85 and 40 kdal. The two larger proteins were identified as the A subunit (gyrA protein) and the B subunit (gyrB protein) of DNA gyrase topoisomerase...
متن کاملA single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.
Binding of the quinolone drug norfloxacin to gyrase and DNA has been investigated. We have detected binding to gyrase-DNA complex but find no significant binding to either gyrase or DNA alone. Enzyme containing gyrase A protein with the mutation Ser-83 to Trp (conferring quinolone resistance) showed greatly reduced drug binding.
متن کاملCrystallization and preliminary crystallographic analysis of the DNA gyrase B protein from B. stearothermophilus.
DNA gyrase B (GyrB) from B. stearothermophilus has been crystallized in the presence of the non-hydrolyzable ATP analogue, 5'-adenylyl-beta-gamma-imidodiphosphate (ADPNP), by the dialysis method. A complete native data set to 3.7 A has been collected from crystals which belonged to the cubic space group I23 with unit-cell dimension a = 250.6 A. Self-rotation function analysis indicates the posi...
متن کاملTryptic fragments of the Escherichia coli DNA gyrase A protein.
Treatment of the Escherichia coli DNA gyrase A protein with trypsin generates two large fragments which are stable to further digestion. The molecular masses of these fragments are 64 and 33 kDa, and they are shown to be derived from the N terminus and the C terminus of the A protein, respectively. These fragments could represent structural and/or functional domains within the A subunit of DNA ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1979
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.76.12.6289