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Relevant bibliographies by topics / DNA Gyrase DNA Gyrase DNA Replication DNA

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Academic literature on the topic 'DNA Gyrase DNA Gyrase DNA Replication DNA'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "DNA Gyrase DNA Gyrase DNA Replication DNA"

1

Hashimi, Saeed M., Melisa K. Wall, Andrew B. Smith, Anthony Maxwell, and Robert G. Birch. "The Phytotoxin Albicidin is a Novel Inhibitor of DNA Gyrase." Antimicrobial Agents and Chemotherapy 51, no. 1 (January 2007): 181–87. http://dx.doi.org/10.1128/aac.00918-06.

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ABSTRACT Xanthomonas albilineans produces a family of polyketide-peptide compounds called albicidins which are highly potent antibiotics and phytotoxins as a result of their inhibition of prokaryotic DNA replication. Here we show that albicidin is a potent inhibitor of the supercoiling activity of bacterial and plant DNA gyrases, with 50% inhibitory concentrations (40 to 50 nM) less than those of most coumarins and quinolones. Albicidin blocks the religation of the cleaved DNA intermediate during the gyrase catalytic sequence and also inhibits the relaxation of supercoiled DNA by gyrase and topoisomerase IV. Unlike the coumarins, albicidin does not inhibit the ATPase activity of gyrase. In contrast to the quinolones, the albicidin concentration required to stabilize the gyrase cleavage complex increases 100-fold in the absence of ATP. The slow peptide poisons microcin B17 and CcdB also access ATP-dependent conformations of gyrase to block religation, but in contrast to albicidin, they do not inhibit supercoiling under routine assay conditions. Some mutations in gyrA, known to confer high-level resistance to quinolones or CcdB, confer low-level resistance or hypersensitivity to albicidin in Escherichia coli. Within the albicidin biosynthesis region in X. albilineans is a gene encoding a pentapeptide repeat protein designated AlbG that binds to E. coli DNA gyrase and that confers a sixfold increase in the level of resistance to albicidin in vitro and in vivo. These results demonstrate that DNA gyrase is the molecular target of albicidin and that X. albilineans encodes a gyrase-interacting protein for self-protection. The novel features of the gyrase-albicidin interaction indicate the potential for the development of new antibacterial drugs.

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Hirsch, Jana, and Dagmar Klostermeier. "What makes a type IIA topoisomerase a gyrase or a Topo IV?" Nucleic Acids Research 49, no. 11 (April 27, 2021): 6027–42. http://dx.doi.org/10.1093/nar/gkab270.

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Abstract Type IIA topoisomerases catalyze a variety of different reactions: eukaryotic topoisomerase II relaxes DNA in an ATP-dependent reaction, whereas the bacterial representatives gyrase and topoisomerase IV (Topo IV) preferentially introduce negative supercoils into DNA (gyrase) or decatenate DNA (Topo IV). Gyrase and Topo IV perform separate, dedicated tasks during replication: gyrase removes positive supercoils in front, Topo IV removes pre-catenanes behind the replication fork. Despite their well-separated cellular functions, gyrase and Topo IV have an overlapping activity spectrum: gyrase is also able to catalyze DNA decatenation, although less efficiently than Topo IV. The balance between supercoiling and decatenation activities is different for gyrases from different organisms. Both enzymes consist of a conserved topoisomerase core and structurally divergent C-terminal domains (CTDs). Deletion of the entire CTD, mutation of a conserved motif and even by just a single point mutation within the CTD converts gyrase into a Topo IV-like enzyme, implicating the CTDs as the major determinant for function. Here, we summarize the structural and mechanistic features that make a type IIA topoisomerase a gyrase or a Topo IV, and discuss the implications for type IIA topoisomerase evolution.

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Aedo, Sandra, and Yuk-Ching Tse-Dinh. "Isolation and Quantitation of Topoisomerase Complexes Accumulated on Escherichia coli Chromosomal DNA." Antimicrobial Agents and Chemotherapy 56, no. 11 (August 6, 2012): 5458–64. http://dx.doi.org/10.1128/aac.01182-12.

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ABSTRACTDNA topoisomerases are important targets in anticancer and antibacterial therapy because drugs can initiate cell death by stabilizing the transient covalent topoisomerase-DNA complex. In this study, we employed a method that uses CsCl density gradient centrifugation to separate unbound from DNA-bound GyrA/ParC inEscherichia colicell lysates after quinolone treatment, allowing antibody detection and quantitation of the covalent complexes on slot blots. Using these procedures modified from thein vivocomplexes of enzyme (ICE) bioassay, we found a correlation between gyrase-DNA complex formation and DNA replication inhibition at bacteriostatic (1× MIC) norfloxacin concentrations. Quantitation of the number of gyrase-DNA complexes perE. colicell permitted an association between cell death and chromosomal gyrase-DNA complex accumulation at norfloxacin concentrations greater than 1× MIC. When comparing levels of gyrase-DNA complexes to topoisomerase IV-DNA complexes in the absence of drug, we observed that the gyrase-DNA complex level was higher (∼150-fold) than that of the topoisomerase IV-DNA complex. In addition, levels of gyrase and topoisomerase IV complexes reached a significant increase after 30 min of treatment at 1× and 1.7× MIC, respectively. These results are in agreement with gyrase being the primary target for quinolones inE. coli. We further validated the utility of this method for the study of topoisomerase-drug interactions in bacteria by showing the gyrase covalent complex reversibility after removal of the drug from the medium, and the resistant effect of the Ser83LeugyrAmutation on accumulation of gyrase covalent complexes on chromosomal DNA.

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Hiasa, Hiroshi, and Molly E. Shea. "DNA Gyrase-mediated Wrapping of the DNA Strand Is Required for the Replication Fork Arrest by the DNA Gyrase-Quinolone-DNA Ternary Complex." Journal of Biological Chemistry 275, no. 44 (August 16, 2000): 34780–86. http://dx.doi.org/10.1074/jbc.m001608200.

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5

Fournier, Bénédicte, Xilin Zhao, Tao Lu, Karl Drlica, and David C. Hooper. "Selective Targeting of Topoisomerase IV and DNA Gyrase in Staphylococcus aureus: Different Patterns of Quinolone- Induced Inhibition of DNA Synthesis." Antimicrobial Agents and Chemotherapy 44, no. 8 (August 1, 2000): 2160–65. http://dx.doi.org/10.1128/aac.44.8.2160-2165.2000.

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ABSTRACT The effect of quinolones on the inhibition of DNA synthesis inStaphylococcus aureus was examined by using single resistance mutations in parC or gyrA to distinguish action against gyrase or topoisomerase IV, respectively. Norfloxacin preferentially attacked topoisomerase IV and blocked DNA synthesis slowly, while nalidixic acid targeted gyrase and inhibited replication rapidly. Ciprofloxacin exhibited an intermediate response, consistent with both enzymes being targeted. The absence of RecA had little influence on target choice by this assay, indicating that differences in rebound (repair) DNA synthesis were not responsible for the results. At saturating drug concentrations, norfloxacin and a gyrA mutant were used to show that topoisomerase IV-norfloxacin-cleaved DNA complexes are distributed on the S. aureus chromosome at intervals of about 30 kbp. If cleaved complexes block DNA replication, as indicated by previous work, such close spacing of topoisomerase-quinolone-DNA complexes should block replication rapidly (replication forks are likely to encounter a cleaved complex within a minute). Thus, the slow inhibition of DNA synthesis at growth-inhibitory concentrations suggests that a subset of more distantly distributed complexes is physiologically relevant for drug action and is unlikely to be located immediately in front of the DNA replication fork.

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Pato, M. L., and M. Banerjee. "Replacement of the Bacteriophage Mu Strong Gyrase Site and Effect on Mu DNA Replication." Journal of Bacteriology 181, no. 18 (September 15, 1999): 5783–89. http://dx.doi.org/10.1128/jb.181.18.5783-5789.1999.

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ABSTRACT The bacteriophage Mu strong gyrase site (SGS) is required for efficient replicative transposition and functions by promoting the synapsis of prophage termini. To look for other sites which could substitute for the SGS in promoting Mu replication, we have replaced the SGS in the middle of the Mu genome with fragments of DNA from various sources. A central fragment from the transposing virus D108 allowed efficient Mu replication and was shown to contain a strong gyrase site. However, neither the strong gyrase site from the plasmid pSC101 nor the major gyrase site from pBR322 could promote efficient Mu replication, even though the pSC101 site is a stronger gyrase site than the Mu SGS as assayed by cleavage in the presence of gyrase and the quinolone enoxacin. To look for SGS-like sites in the Escherichia coli chromosome which might be involved in organizing nucleoid structure, fragments of E. coli chromosomal DNA were substituted for the SGS: first, repeat sequences associated with gyrase binding (bacterial interspersed mosaic elements), and, second, random fragments of the entire chromosome. No fragments were found that could replace the SGS in promoting efficient Mu replication. These results demonstrate that the gyrase sites from the transposing phages possess unusual properties and emphasize the need to determine the basis of these properties.

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Dar, Mohd Ashraf, Atul Sharma, Neelima Mondal, and Suman Kumar Dhar. "Molecular Cloning of Apicoplast-Targeted Plasmodium falciparum DNA Gyrase Genes: Unique Intrinsic ATPase Activity and ATP-Independent Dimerization of PfGyrB Subunit." Eukaryotic Cell 6, no. 3 (January 12, 2007): 398–412. http://dx.doi.org/10.1128/ec.00357-06.

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ABSTRACT DNA gyrase, a typical type II topoisomerase that can introduce negative supercoils in DNA, is essential for replication and transcription in prokaryotes. The apicomplexan parasite Plasmodium falciparum contains the genes for both gyrase A and gyrase B in its genome. Due to the large sizes of both proteins and the unusual codon usage of the highly AT-rich P. falciparum gyrA (PfgyrA) and PfgyrB genes, it has so far been impossible to characterize these proteins, which could be excellent drug targets. Here, we report the cloning, expression, and functional characterization of full-length PfGyrB and functional domains of PfGyrA. Unlike Escherichia coli GyrB, PfGyrB shows strong intrinsic ATPase activity and follows a linear pattern of ATP hydrolysis characteristic of dimer formation in the absence of ATP analogues. These unique features have not been reported for any known gyrase so far. The PfgyrB gene complemented the E. coli gyrase temperature-sensitive strain, and, together with the N-terminal domain of PfGyrA, it showed typical DNA cleavage activity. Furthermore, PfGyrA contains a unique leucine heptad repeat that might be responsible for dimerization. These results confirm the presence of DNA gyrase in eukaryotes and confer great potential for drug development and organelle DNA replication in the deadliest human malarial parasite, P. falciparum.

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Rovinskiy, Nikolay, Andrews Agbleke, Olga Chesnokova, and N. Higgins. "Supercoil Levels in E. coli and Salmonella Chromosomes Are Regulated by the C-Terminal 35–38 Amino Acids of GyrA." Microorganisms 7, no. 3 (March 15, 2019): 81. http://dx.doi.org/10.3390/microorganisms7030081.

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Prokaryotes have an essential gene—gyrase—that catalyzes negative supercoiling of plasmid and chromosomal DNA. Negative supercoils influence DNA replication, transcription, homologous recombination, site-specific recombination, genetic transposition and sister chromosome segregation. Although E. coli and Salmonella Typhimurium are close relatives with a conserved set of essential genes, E. coli DNA has a supercoil density 15% higher than Salmonella, and E. coli cannot grow at the supercoil density maintained by wild type (WT) Salmonella. E. coli is addicted to high supercoiling levels for efficient chromosomal folding. In vitro experiments were performed with four gyrase isoforms of the tetrameric enzyme (GyrA2:GyrB2). E. coli gyrase was more processive and faster than the Salmonella enzyme, but Salmonella strains with chromosomal swaps of E. coli GyrA lost 40% of the chromosomal supercoil density. Reciprocal experiments in E. coli showed chromosomal dysfunction for strains harboring Salmonella GyrA. One GyrA segment responsible for dis-regulation was uncovered by constructing and testing GyrA chimeras in vivo. The six pinwheel elements and the C-terminal 35–38 acidic residues of GyrA controlled WT chromosome-wide supercoiling density in both species. A model of enzyme processivity modulated by competition between DNA and the GyrA acidic tail for access to β-pinwheel elements is presented.

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Hardy, Christine D., and Nicholas R. Cozzarelli. "Alteration of Escherichia coli Topoisomerase IV to Novobiocin Resistance." Antimicrobial Agents and Chemotherapy 47, no. 3 (March 2003): 941–47. http://dx.doi.org/10.1128/aac.47.3.941-947.2003.

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ABSTRACT DNA gyrase and topoisomerase IV (topo IV) are the two essential type II topoisomerases of Escherichia coli. Gyrase is responsible for maintaining negative supercoiling of the bacterial chromosome, whereas topo IV's primary role is in disentangling daughter chromosomes following DNA replication. Coumarins, such as novobiocin, are wide-spectrum antimicrobial agents that primarily interfere with DNA gyrase. In this work we designed an alteration in the ParE subunit of topo IV at a site homologous to that which confers coumarin resistance in gyrase. This parE mutation renders the encoded topo IV approximately 40-fold resistant to inhibition by novobiocin in vitro and imparts a similar resistance to inhibition of topo IV-mediated relaxation of supercoiled DNA in vivo. We conclude that topo IV is a secondary target of novobiocin and that it is very likely to be inhibited by the same mechanism as DNA gyrase.

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Pang, Zhenhua, Ray Chen, Dipankar Manna, and N. Patrick Higgins. "A Gyrase Mutant with Low Activity Disrupts Supercoiling at the Replication Terminus." Journal of Bacteriology 187, no. 22 (November 15, 2005): 7773–83. http://dx.doi.org/10.1128/jb.187.22.7773-7783.2005.

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ABSTRACT When a mutation in an essential gene shows a temperature-sensitive phenotype, one usually assumes that the protein is inactive at nonpermissive temperature. DNA gyrase is an essential bacterial enzyme composed of two subunits, GyrA and GyrB. The gyrB652 mutation results from a single base change that substitutes a serine residue for arginine 436 (R436-S) in the GyrB protein. At 42°C, strains with the gyrB652 allele stop DNA replication, and at 37°C, such strains grow but have RecA-dependent SOS induction and show constitutive RecBCD-dependent DNA degradation. Surprisingly, the GyrB652 protein is not inactive at 42°C in vivo or in vitro and it doesn't directly produce breaks in chromosomal DNA. Rather, this mutant has a low k cat compared to wild-type GyrB subunit. With more than twice the normal mean number of supercoil domains, this gyrase hypomorph is prone to fork collapse and topological chaos near the terminus of DNA replication.

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Dissertations / Theses on the topic "DNA Gyrase DNA Gyrase DNA Replication DNA"

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Pang, Zhenhua. "Surveying the chromosomal supercoiling levels in rapidly growing wild type and gyrase mutant strains of Salmonella enterica serovar Typhimurium with [gamma delta] resolvase-mediated recombination assay." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2007r/pang.pdf.

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Jolly, Samson M. "Thermus thermophilus Argonaute Functions in the Completion of DNA Replication." eScholarship@UMMS, 2020. https://escholarship.umassmed.edu/gsbs_diss/1096.

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Argonautes (AGOs) are present in all domains of life. Like their eukaryotic counterparts, archaeal and eubacterial AGOs adopt a similar global architecture and bind small nucleic acids. In many eukaryotes, AGOs, guided by short RNA sequences, defend cells against transposons and viruses. In the eubacterium Thermus thermophilus, the DNA-guided Argonaute TtAgo defends against transformation by DNA plasmids. We find that TtAgo also participates in DNA replication. In vivo, TtAgo binds 15–18 nt DNA guides derived from the chromosomal region where replication terminates, and TtAgo complexed to short DNA guides enhances target finding and prefers to bind targets with full complementarity. Additionally, TtAgo associates with proteins known to act in DNA replication. When gyrase, the sole T. thermophilus type II topoisomerase, is inhibited, TtAgo allows the bacterium to finish replicating its circular genome. In contrast, loss of both gyrase and TtAgo activity slows growth and produces long, segmented filaments in which the individual bacteria are linked by DNA. Furthermore, wild-type T. thermophilus outcompetes an otherwise isogenic strain lacking TtAgo. Finally, at physiologic temperature in vitro, we find TtAgo possesses highest affinity for fully complementary targets. We propose that terminus-derived guides binding in such a fashion localize TtAgo, and that the primary role of TtAgo is to help T. thermophilus disentangle the catenated circular chromosomes generated by DNA replication.

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Evans-Roberts, Katherine Mary. "DNA gyrase of 'Arabidopsis thaliana'." Thesis, University of East Anglia, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.443072.

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Tingey, Andrew Philip. "Strand passage in DNA gyrase." Thesis, University of Leicester, 1996. http://hdl.handle.net/2381/35173.

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DNA gyrase, a type II topoisomerase, catalyses the introduction of negative supercoils into closed-circular DNA, using the energy from ATP hydrolysis. The reaction mechanism involves the breakage of one DNA double strand (the DNA gate) and the passing of another DNA strand (the passage helix) through that break and finally the re-sealing of the DNA gate. The strand-passage reaction was studied by the use of novel DNA substrates and by site-directed mutagenesis of one of the gyrase proteins. The DNA substrates were used to attempt to define the DNA segments used by the enzyme as the DNA gate and passage helix in a catenation reaction. This was achieved by using oligonucleotides to form partial duplex regions in single-stranded DNA. A high-affinity gyrase cleavage site from the plasmid pBR322 was cloned into M13mpl8 and generated both the single and double-stranded circular forms of the molecule (MAT1). It was shown that gyrase could form a specific DNA gate in a short duplex region in single-stranded MAT1 when quinolone drugs were present. This DNA gate was much smaller than that normally utilised by the enzyme. The catenation and decatenation reactions were examined in detail with normal duplex substrates; reactions using a non-hydrolysable ATP analogue gave different results to those previously reported for the eukaryotic homologue of gyrase, indicating a possible mechanistic difference between the enzymes. Conditions under which the partial duplex substrates would be catenated were not found. Site-directed mutagenesis was used to alter arginine residues thought to interact with the passage helix during the reaction cycle. Assays of the mutant protein revealed that supercoiling activity was markedly reduced, but that partial activities of gyrase, such as the ATPase and DNA cleavage reactions, were close to wild-type levels.

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Williams, Nicola Louise. "Protein gates in DNA gyrase." Thesis, University of Leicester, 1999. http://hdl.handle.net/2381/29641.

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DNA gyrase is a molecular machine comprising a series of protein gates. The opening and closing of these gates enables the passage of one segment of double-stranded DNA (the T segment) through a transient break in another (the G segment). We have blocked the passage of DNA through each of three dimer interfaces within gyrase and investigated the effects on gyrase mechanism. This has been achieved by cross-linking novel cysteine residues on either side of the dimer interface, or trapping the dimer interface in a closed conformation using a non-hydrolysable ATP analogue. Cross-linking a pair of novel cysteine residues on either side of the bottom dimer interface of DNA gyrase blocks catalytic supercoiling. Limited strand passage is allowed, but T-segment release is prevented. In contrast, ATP-independent relaxation of negatively supercoiled DNA is completely abolished, suggesting that T-segment entry via the bottom gate is blocked. These findings support a two-gate model for supercoiling in by DNA gyrase and suggest that relaxation by gyrase is the reversal of supercoiling. Cross-linking a truncated version of gyrase, (A642B2) that lacks the DNA wrapping domains, does not block ATP-dependent relaxation. This indicates that passage of DNA through the bottom dimer interface is not essential for this reaction. Using a similar approach, we have locked the DNA gate of gyrase using cysteine cross-linking. We show that this locked-gate mutant can bind quinolone drugs and perform DNA cleavage. However, locking the DNA gate prevents strand passage and the ability of DNA to stimulate ATP hydrolysis.

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Noble, Christian Guy. "DNA gyrase : the molecular enzymology of the DNA cleavage reaction." Thesis, University of East Anglia, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.251437.

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Ali, Janid Asghar. "The ATPase reaction of DNA gyrase." Thesis, University of Leicester, 1993. http://hdl.handle.net/2381/35097.

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Purification of the DNA gyrase B protein consistently led to two contaminating bands of 47kDa and 43kDa molecular masses. These were found to be the C- and N-terminal fragments of GyrB. The specific supercoiling activity of GyrB was found to be consistently lower than the specific supercoiling activity of GyrA. This was due to about 90% of GyrB being in an uncoupled form. The uncoupled GyrB was found to have a relatively high ATPase activity, therefore an in-depth kinetic study on DNA gyrase was not possible. Kinetic studies were carried out on the 43kDa protein, which is a cloned N-terminal fragment of GyrB. The 43kDa protein was found to hydrolyse ATP at a relatively low rate, with 10 muM 43kDa having and apparent kcat of 0.01 s-1, and 20 muM a kcat of 0.02 s-1. A greater than first order dependence of rate upon 43kDa concentration was observed in the concentration range of 2-40 muM. Hyperbolic type kinetics were observed at constant 43kDa concentration (5, 10, 20 and 40 ?M) for the rate with respect to ATP concentration. A model which was found to be consistent with molecular weight studies and the kinetic data has been proposed. The 43kDa monomer can bind ATP but is not competent to hydrolyse ATP. Hydrolysis can only occur in the context of a 43kDa2ATP2 dimer, which leads to the collapse of the dimer into monomers and release of products. The rate limiting step at the protein concentration range used is the dimerisation step. Novobiocin and coumermycin inhibit the ATPase reaction, with novobiocin binding at a stoichiometry of 1 novobiocin molecule to 1 43kDa monomer and coumermycin binding with a stoichiometry of 1 molecule to two molecules of 43kDa protein. The inhibition by coumarin drugs appears non-competitive. ADPNP binding to the 43kDa protein was found to be slow, with a second order rate constant of 0.86 M-1s-1 to 9.9 M-1s-1. ADPNP seems to bind with stoichiometries varying from 2 per 43kDa dimer to 1 per 43kDa dimer. ATP and ADP inhibit the amount of ADPNP bound, with ATP having no effect on the rate of ADPNP binding and ADP decreasing the rate of ADPNP binding. Novobiocin and coumermycin inhibit ADPNP binding to the 43kDa protein. ADPNP dissociates from the 43kDa protein at a very slow rate, with a half life of about 8 days. ATP and ADP have little effect on this rate. However high concentrations of novobiocin (10-100 mM) dramatically increase the rate of ADPNP dissociation from the 43kDa protein, indicating different coumarin and nucleotide binding sites.

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Tsai, Francis T. F. "Crystallographic studies of DNA gyrase B protein." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390473.

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Hallett, Paul. "Studies on DNA gyrase and quinolone drugs." Thesis, University of Leicester, 1990. http://hdl.handle.net/2381/35242.

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A study has been conducted aimed at the generation and characterisation of mutations in the Escherichia coli gyrA gene, resistant to the quinolone group of antibacterial agents. Preliminary studies on quinolone-resistant mutants of strains that over-express the DNA gyrA gene, revealed the over-production of a 60 KDa protein which was partially purified. This 60 KDa protein was found to be similar, but not identical to the E. coli heat shock protein GroEL. The gyrA gene has been recloned in the 8.0 kb plasmid pPH3, which contains the gene under the stringent control of the hybrid tac promoter. The E. coli strain JMtacA containing pPH3 exhibits no expression of the gyrA gene in the absence of the inducer (IPTG), but over-produces the protein at greater than 20% of the total soluble cell protein after induction. The optimisation and purification of the GyrA subunit from JMtacA is also described. A fragment was subjected to site-directed mutagenesis which contained the TCG codon for serine-83, which was mutated to alanine (GCG). The mutant showed a 15x increase in MIC50 compared to wild-type. The mutated GyrA subunit was over-produced, complexed with wild-type GyrB subunit and used in various assays for reactions performed by DNA gyrase. The ID50 was determined for supercoiling, decatenation, relaxation of negatively supercoiled DNA, and cleavage of supercoiled DNA. The cleavage reaction mediated by Ca++ was also investigated. The technique of gap-misrepair mutagenesis, geared to the generation of single, random point mutations on a plasmid was also used on the plasmid pPH3, to generate a quinolone-resistant mutant of the gyrA gene. The mutant isolated (GMIOO) was also over-produced and compared to wild-type in various assays. The mutation was determined by DNA sequencing to be glutamine-106 to arginine.

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Mitelheiser, Sylvain. "DNA gyrase, quinolone drugs and supercoiling mechanism." Thesis, University of East Anglia, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.423811.

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Books on the topic "DNA Gyrase DNA Gyrase DNA Replication DNA"

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Thornton, Mark. Intracellular localisation of DNA Gyrase subunits GyrA and GyrB using immunogold labelling inEscherichia coli. Manchester: University of Manchester, 1995.

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2

International Symposium on DNA Topoisomerases in Chemotherapy (1991 Nagoya-shi, Japan). Molecular biology of DNA topoisomerases and its application to chemotherapy: Proceedings of the International Symposium on DNA Topoisomerases in Chemotherapy, Nagoya, Japan, November 18-20, 1991 (ISTOP 1991). Boca Raton: CRC Press, 1993.

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Book chapters on the topic "DNA Gyrase DNA Gyrase DNA Replication DNA"

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Gooch, Jan W. "DNA Gyrase." In Encyclopedic Dictionary of Polymers, 888. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13588.

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Khan, Tabassum, and Kaksha Sankhe. "DNA Gyrase Inhibitors." In Encyclopedia of Molecular Pharmacology, 1–8. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-21573-6_141-1.

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Luan, Gan, and Karl Drlica. "Fluoroquinolone-Gyrase-DNA Cleaved Complexes." In Methods in Molecular Biology, 269–81. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7459-7_19.

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Wigley, D. B. "Structure and Mechanism of DNA Gyrase." In Nucleic Acids and Molecular Biology, 165–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79488-9_8.

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Bryskier, A. "DNA Gyrase Inhibitors Other Than Fluoroquinolones." In Antimicrobial Agents, 789–97. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815929.ch27.

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Martínez-García, Belén, Antonio Valdés, Joana Segura, Silvia Dyson, Ofelia Díaz-Ingelmo, and Joaquim Roca. "Electrophoretic Analysis of the DNA Supercoiling Activity of DNA Gyrase." In Methods in Molecular Biology, 291–300. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8556-2_15.

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Crumplin, G. C. "Molecular Effects of 4-Quinolones upon DNA Gyrase: DNA Systems." In The 4-Quinolones: Anti Bacterial Agents in Vitro, 53–68. London: Springer London, 1990. http://dx.doi.org/10.1007/978-1-4471-3449-7_5.

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Elwell, L. P., L. M. Walton, J. M. Besterman, and A. Hudson. "Use of an In Vitro DNA Strand-Breakage Assay to Monitor Compound Interactions with DNA Gyrase." In The 4-Quinolones: Anti Bacterial Agents in Vitro, 87–102. London: Springer London, 1990. http://dx.doi.org/10.1007/978-1-4471-3449-7_7.

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Fisher, L. Mark, and Xiao-Su Pan. "Methods to Assay Inhibitors of DNA Gyrase and Topoisomerase IV Activities." In Methods In Molecular Medicine™, 11–23. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-246-5_2.

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Racko, Dusan, Fabrizio Benedetti, Julien Dorier, Yannis Burnier, and Andrzej Stasiak. "Molecular Dynamics Simulation of Supercoiled, Knotted, and Catenated DNA Molecules, Including Modeling of Action of DNA Gyrase." In The Bacterial Nucleoid, 339–72. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7098-8_24.

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Reports on the topic "DNA Gyrase DNA Gyrase DNA Replication DNA"

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D'Ambrozio, Jonathan A. Insights into the Enhanced in vivo Fitness of Neisseria gonorrhoeae Driven by a Fluoroquinolone Resistance-Conferring Mutant DNA Gyrase. Fort Belvoir, VA: Defense Technical Information Center, January 2015. http://dx.doi.org/10.21236/ad1012700.

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