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Roca JR, Wang JC. The capture of a DNA double helix by an ATP-dependent protein clamp: a key step in DNA transport by type II DNA topoisomerases. Cell. 71:1992;833-840.
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Roca, J.R.1
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Ali JA, Orphanides G, Maxwell A. Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein. Biochemistry. 34:1995;9801-9808.
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Ali, J.A.1
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0030045003
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Structure at 2.7 Å of a 92 K yeast topoisomerase II fragment
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of outstanding interest. This paper presents the first structure of a cleavage-competent fragment of a type II topoisomerase. The architectural arrangement of the dimer suggests a model for how duplex transport can occur.
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of outstanding interest Berger JM, Gamblin SJ, Harrison SC, Wang JC. Structure at 2.7 Å of a 92 K yeast topoisomerase II fragment. Nature. 379:1996;225-232 This paper presents the first structure of a cleavage-competent fragment of a type II topoisomerase. The architectural arrangement of the dimer suggests a model for how duplex transport can occur.
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Nature
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Berger, J.M.1
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Schultz, S.C.1
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0000301456
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Crystal structure of the breakage - Reunion domain of DNA gyrase
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of outstanding interest. This paper describes the structure of a GyrA fragment homologous to the C-terminal two-thirds of the topo II structure, demonstrating an alternative conformational state for the DNA binding or cleavage domain.
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of outstanding interest Cabral JHM, Jackson AP, Smith CV, Shikotra N, Maxwell A, Liddington RC. Crystal structure of the breakage - reunion domain of DNA gyrase. Nature. 388:1997;903-906 This paper describes the structure of a GyrA fragment homologous to the C-terminal two-thirds of the topo II structure, demonstrating an alternative conformational state for the DNA binding or cleavage domain.
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Nature
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Cabral, J.H.M.1
Jackson, A.P.2
Smith, C.V.3
Shikotra, N.4
Maxwell, A.5
Liddington, R.C.6
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Nuclease protection by Drosophila topoisomerase II: Enzyme/DNA contacts at the strong topoisomerase II cleavage sites
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Lee MP, Sander M, Hsieh T. Nuclease protection by Drosophila topoisomerase II: enzyme/DNA contacts at the strong topoisomerase II cleavage sites. J Biol Chem. 264:1989;21779-21787.
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Lee, M.P.1
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Evidence for a conformational change in the DNA gyrase-DNA complex from hydroxyl radical footprinting
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Orphanides G, Maxwell A. Evidence for a conformational change in the DNA gyrase-DNA complex from hydroxyl radical footprinting. Nucleic Acids Res. 22:1994;1567-1575.
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Peng H, Marians KJ. The interaction of Escherichia coli topoisomerase IV with DNA. J Biol Chem. 270:1995;25286-25290.
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Gmunder H, Kuratli K, Keck W. In the presence of subunit A inhibitors DNA gyrase cleaves DNA fragments as short as 20 bp at specific sites. Nucleic Acids Res. 25:1997;604-611.
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Gmunder, H.1
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14
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Characterization of topoisomerase II - DNA interaction and identification of a DNA-binding domain by ultraviolet laser crosslinking
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Hung F, Luo D, Sauve D, Muller M, Roberge M. Characterization of topoisomerase II - DNA interaction and identification of a DNA-binding domain by ultraviolet laser crosslinking. FEBS Lett. 380:1996;127-132.
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Hung, F.1
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Roberge, M.5
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15
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0030707827
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Footprinting of yeast DNA topoisomerase II lysyl side chains involved in substrate binding and interdomainal interations
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of special interest. This paper describes a number of experiments that map the position of protein - DNA interactions and that demonstrate that both intramolecular contacts and the global conformation change during substrate binding.
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of special interest Li W, Wang J. Footprinting of yeast DNA topoisomerase II lysyl side chains involved in substrate binding and interdomainal interations. J Biol Chem. 272:1997;31190-31195 This paper describes a number of experiments that map the position of protein - DNA interactions and that demonstrate that both intramolecular contacts and the global conformation change during substrate binding.
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Li, W.1
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The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein
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Reece RJ, Maxwell A. The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Nucleic Acids Res. 19:1991;1399-1405.
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Kirkegaard K, Wang JC. Mapping the topography of DNA wrapped around gyrase by nucleolytic and chemical probing of complexes of unique DNA sequences. Cell. 23:1981;721-729.
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19
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0029955899
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Conversion of DNA gyrase into a conventional type II topoisomerase
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of special interest. The authors show that the C-terminal DNA-binding domains of the GyrA subunit are primarily responsible for the unique supercoiling abilities of gyrase.
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of special interest Kampranis S, Maxwell A. Conversion of DNA gyrase into a conventional type II topoisomerase. Proc Natl Acad Sci USA. 93:1996;14416-14421 The authors show that the C-terminal DNA-binding domains of the GyrA subunit are primarily responsible for the unique supercoiling abilities of gyrase.
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Kampranis, S.1
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Bates AD, O'Dea MH, Gellert M. Energy coupling in Escherichia coli DNA gyrase: the relationship between nucleotide binding, strand passage, and DNA supercoiling. Biochemistry. 35:1996;1408-1416.
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Bates, A.D.1
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Ullsperger C, Cozzarelli N. Contrasting enzymatic activities of topoisomerase IV and DNA gyrase from Escherichia coli. J Biol Chem. 271:1996;1549-1555.
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Ullsperger, C.1
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Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase
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Tingey AP, Maxwell A. Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase. Nucleic Acids Res. 24:1996;4868-4873.
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Tingey, A.P.1
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Roca J, Berger JM, Wang JC. On the simultaneous binding of eukaryotic DNA topoisomerase II to a pair of double-stranded DNA helices. J Biol Chem. 268:1993;14250-14255.
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27
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0029897384
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Structure and conformational changes of DNA topoisomerase II visualized by electron microscopy
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of special interest. This paper presents striking visual evidence of the conformational changes that occur upon nucleotide binding and suggests where DNA is bound by the enzyme.
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of special interest Schultz P, Olland S, Oudet P, Hancock R. Structure and conformational changes of DNA topoisomerase II visualized by electron microscopy. Proc Natl Acad Sci USA. 93:1996;5936-5940 This paper presents striking visual evidence of the conformational changes that occur upon nucleotide binding and suggests where DNA is bound by the enzyme.
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Schultz, P.1
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28
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Study of yeast DNA topoisomerase and its truncation derivatives by transmission electron microscopy
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of special interest. This paper examines the structure of a number of topoisomerase truncation variants, building a picture of the quarternary arrangement of an intact type II enzyme.
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of special interest Benedetti P, Silvestri A, Fiorani P, Wang JC. Study of yeast DNA topoisomerase and its truncation derivatives by transmission electron microscopy. J Biol Chem. 272:1997;12132-12137 This paper examines the structure of a number of topoisomerase truncation variants, building a picture of the quarternary arrangement of an intact type II enzyme.
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40
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0030758268
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Simplification of DNA topology below equilibrium values by type II topoisomerases
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of special interest. This paper presents the striking observation that type II enzymes can push the topological states accessible to DNA away from thermodynamic equilibrium.
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of special interest Rybenkov V, Ullsperger C, Vologodskii A, Cozzarelli NR. Simplification of DNA topology below equilibrium values by type II topoisomerases. Science. 277:1997;690-693 This paper presents the striking observation that type II enzymes can push the topological states accessible to DNA away from thermodynamic equilibrium.
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42
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0030987132
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An atypical topoisomerase II from archaea with implications for meiotic recombination
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of outstanding interest. The authors present the first evidence of a new type of enzyme that can carry out the complex type II topoisomerase DNA transport reaction, yet so far appears to be unrelated to classic type II proteins.
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of outstanding interest Bergerat A, de Massy B, Gadelle D, Varoutas P-C, Nicolas A, Forterre P. An atypical topoisomerase II from archaea with implications for meiotic recombination. Nature. 386:1997;414-416 The authors present the first evidence of a new type of enzyme that can carry out the complex type II topoisomerase DNA transport reaction, yet so far appears to be unrelated to classic type II proteins.
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Nature
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Bergerat, A.1
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Gadelle, D.3
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