Search Results - "HIASA, H"

DNA Strand Cleavage Is Required for Replication Fork Arrest by a Frozen Topoisomerase-Quinolone-DNA Ternary Complex by Hiasa, H, Yousef, D O, Marians, K J

“…The formation of a topoisomerase-quinolone-DNA ternary complex leads to cell death. We show here that an active strand breakage and reunion activity is…”
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Decatenating activity of Escherichia coli DNA gyrase and topoisomerases I and III during oriC and pBR322 DNA replication in vitro by HIASA, H, DIGATE, R. J, MARIANS, K. J

“…oriC and pBR322 DNA replication, reconstituted with purified replication proteins, has been used to study the functional activities of Escherichia coli…”
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Primase couples leading- and lagging-strand DNA synthesis from oriC by HIASA, H, MARIANS, K. J

“…Coupling of leading- and lagging-strand DNA synthesis at replication forks formed at Escherichia coli oriC has been studied in vitro using a replication system…”
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Topoisomerase III, but not topoisomerase I, can support nascent chain elongation during theta-type DNA replication by Hiasa, H, Marians, K J

“…Topoisomerase III, but not topoisomerase I, could, in the absence of DNA gyrase, support bidirectional DNA replication in an oriC plasmid DNA replication…”
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A ParE−ParC Fusion Protein Is a Functional Topoisomerase by Lavasani, Leela S, Hiasa, Hiroshi

“…Type II topoisomerases are responsible for DNA unlinking during DNA replication and chromosome segregation. Although eukaryotic enzymes are homodimers and…”
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Topoisomerase IV can support oriC DNA replication in vitro by HIASA, H, MARIANS, K. J

“…Escherichia coli has two type II topoisomerases, DNA gyrase and topoisomerase IV (Topo IV). Topo IV is required for the decatenation of the linked daughter…”
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Fis cannot support oriC DNA replication in vitro by Hiasa, H, Marians, K J

“…The effects of the histone-like proteins, HU, IHF, and Fis on DNA replication have been examined in vitro using the oriC and pBR322 DNA replication systems. In…”
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Replicative helicases can translocate through abasic site-induced covalent topoisomerase IV-DNA complexes by Shea, M E, Hiasa, H

“…Some topoisomerase inhibitors trap covalent topoisomerase-DNA complexes as topoisomerase-drug-DNA ternary complexes. Ternary complex formation results in…”
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Differential inhibition of the DNA translocation and DNA unwinding activities of DNA helicases by the Escherichia coli Tus protein by HIASA, H, MARIANS, K. J

“…Binding of the Escherichia coli Tus protein to its cognate nonpalindromic binding site on duplex DNA (a Ter sequence) is sufficient to arrest the progression…”
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Tus prevents overreplication of oriC plasmid DNA by Hiasa, H, Marians, K J

“…Minichromosome plasmid DNA templates containing oriC and two Ter sites, oriented as they are on the Escherichia coli chromosome, have been used to study the…”
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The Glu-84 of the ParC Subunit Plays Critical Roles in Both Topoisomerase IV−Quinolone and Topoisomerase IV−DNA Interactions by Hiasa, Hiroshi

“…DNA gyrase and topoisomerase IV (Topo IV) are cellular targets of quinolone antibacterial drugs. The Ser-80 and the Glu-84 of the ParC subunit have been…”
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Functional Division and Reconstruction of a Plasmid Replication Origin: Molecular Dissection of the oriV of the Broad-Host-Range Plasmid RSF1010 by Honda, Yoichi, Sakai, Hiroshi, Hiasa, Hiroshi, Tanaka, Katsunori, Komano, Tohru, Bagdasarian, Michael

“…Two single-stranded DNA initiation signals (designated ssi) present in the origin of vegetative DNA replication (oriV) of the broad-host-range plasmid RSF1010…”
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The “GyrA-box” Is Required for the Ability of DNA Gyrase to Wrap DNA and Catalyze the Supercoiling Reaction by Kramlinger, Valerie M., Hiasa, Hiroshi

“…DNA gyrase is the only topoisomerase that can introduce negative supercoils into DNA. It is thought that the binding of conventional type II topoisomerases,…”
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Comparative analysis of functional and structural features in the primase-dependent priming signals, G sites, from phages and plasmids by TANAKA, K, ROGI, T, HIASA, H, DENG-MING MIAO, HONDA, Y, NOMURA, N, SAKAI, H, KOMANO, T

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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DNA gyrase and topoisomerase IV: biochemical activities, physiological roles during chromosome replication, and drug sensitivities by Levine, Cindy, Hiasa, Hiroshi, Marians, Kenneth J.

“…DNA gyrase and topoisomerase IV are the two type II topoisomerases present in bacteria. Though clearly related, based on amino acid sequence similarity, they…”
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Replacement of ParC alpha 4 Helix with That of GyrA Increases the Stability and Cytotoxicity of Topoisomerase IV-Quinolone-DNA Ternary Complexes by Pfeiffer, E S, Hiasa, H

“…Replacement of the alpha 4 helix of ParC with that of GyrA increased the stability of topoisomerase IV-quinolone-DNA ternary complexes. This mutant…”
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RecA can stimulate the relaxation activity of topoisomerase I: Molecular basis of topoisomerase-mediated genome-wide transcriptional responses in Escherichia coli by Reckinger, Amy R, Jeong, Kyeong Soo, Khodursky, Arkady B, Hiasa, Hiroshi

“…The superhelicity of the chromosome, which is controlled by DNA topoisomerases, modulates global gene expression. Investigations of transcriptional responses…”
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Mechanism of quinolone action. A drug-induced structural perturbation of the DNA precedes strand cleavage by topoisomerase IV by Marians, K J, Hiasa, H

“…Quinolones are potent broad spectrum antibacterial drugs that target the bacterial type II DNA topoisomerases. Their cytotoxicity derives from their ability to…”
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Characterization of a unique type IA topoisomerase in Bacillus cereus by Li, Zhiyu, Hiasa, Hiroshi, DiGate, Russell

“…Summary Bacillus cereus topoisomerase IIIβ (bcTopo IIIβ) has been cloned, overexpressed and biochemically characterized. This enzyme exhibits 64% and 33%…”
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The RuvAB Branch Migration Complex Can Displace Topoisomerase IV super(.)Quinolone super(.)DNA Ternary Complexes by Shea, ME, Hiasa, H

“…Quinolone antimicrobial drugs target both DNA gyrase and topoisomerase IV (Topo IV) and convert these essential enzymes into cellular poisons. Topoisomerase…”
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