Download DNA Topoisomerase. Enzymology and Drugs Vol.II by Neil Osheroff, Mary-Ann Bjornsti PDF

By Neil Osheroff, Mary-Ann Bjornsti

Starting with the Escherichia coli ? protein, or bacterial DNA topoisomerase I, an ever-increasing variety of enzymes were pointed out that catalyze alterations within the linkage of DNA strands. DNA topoisomerases are ubiquitous in nature and feature been proven to play severe roles in such a lot p- cesses concerning DNA, together with DNA replication, transcription, and rec- bination. those enzymes extra represent the mobile pursuits of a couple of clinically vital antibacterial and anticancer brokers. therefore, extra reviews of DNA topology and DNA topoisomerases are severe to develop our und- status of the fundamental organic procedures required for mobile cycle development, mobilephone department, genomic balance, and improvement. furthermore, those experiences will proceed to supply severe insights into the cytotoxic motion of substances that focus on DNA topoisomerases. Such mechanistic reviews have already performed an immense position within the improvement and scientific software of antimicrobial and chemotherapeutic brokers. the 2 volumes of DNA Topoisomerase Protocols are designed to aid new and verified researchers examine all facets of DNA topology and the functionality of those enzymes. The chapters are written via popular investigators within the box and supply designated historical past info and st- by-step experimental protocols. the themes lined partly I: DNA Topology and Enzymes, variety from precise the way to study numerous points of DNA constitution, from linking quantity, knotting/unknotting, site-specific recombi- tion, and decatenation to the overexpression and purification of bacterial and eukaryotic DNA topoisomerases from numerous telephone platforms and tissues.

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After phenol extraction, the DNA is precipitated and analyzed by agarose gels. Figure 9B shows an increasing electrophoretic mobility as the ratio of reverse gyrase to DNA is increased during the initial incubation. More precise analysis indicates that the DNA becomes more and more negatively supercoiled, suggesting that stoichiometric binding of reverse gyrase induces DNA unwinding. 4. Notes 1. This buffer allows storage of reverse gyrase with the same specific activity for several years. 2. Taking into account the high temperature of the enzymatic incubation, care is taken to avoid evaporation.

10 is described below. 1. 4 µg relaxed pBR322, and various dilutions of the gyrase activity to be assayed (final volume 35 µL). In the case of purified GyrA and GyrB subunits, various dilutions of the subunit to be assayed are made in gyrase dilution buffer (Note 9) (on ice) and added to reaction mix on ice containing an excess (>10 U) of the complementing subunit. 2. 4 µg), ATP (Note 10), complementing subunit (where appropriate), and sterile water to 33 µL. 5-mL Eppendorf tubes on ice, and the gyrase (2 µL) is added.

Wang, J. C. (1996) DNA topoisomerases. Annu. Rev. Biochem. 65, 635–692. 4. Burden, D. A. and Osheroff, N. (1998) Mechanism of action of eukaryotic topoisomerase II and drugs targeted to the enzyme. Biochem. Biophys. Acta. 1400, 139–154. 5. Osheroff, N. (1986) Eukaryotic topoisomerase II. Characterization of enzyme turnover. J. Biol. Chem. 261, 9944–9950. 6. Roca, J. and Wang, J. C. (1992) The capture of a DNA double helix by an ATPdependent protein clamp: a key step in DNA transport by type II DNA topoisomerases.

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