ArticleProceedings of the National Academy of Sciences of the United States of America1999
Similarity in the catalysis of DNA breakage and rejoining by type IA and IIA DNA topoisomerases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Structural insights into the assembly of type IIA topoisomerase DNA cleavage-religation center.Nucleic acids research · 2024Article
- Negative supercoils regulate meiotic crossover patterns in budding yeast.Nucleic acids research · 2022Article
- The Impact of the C-Terminal Region on the Interaction of Topoisomerase II Alpha with Mitotic Chromatin.International journal of molecular sciences · 2019Article
- Synthesis and molecular docking studies of some novel Schiff bases incorporating 6-butylquinolinedione moiety as potential topoisomerase IIβ inhibitors.Royal Society open science · 2018Article
- Structural basis of DNA gyrase inhibition by antibacterial QPT-1, anticancer drug etoposide and moxifloxacin.Nature communications · 2015Article
- Recovery of the poisoned topoisomerase II for DNA religation: coordinated motion of the cleavage core revealed with the microsecond atomistic simulation.Nucleic acids research · 2015Article
- The α isoform of topoisomerase II is required for hypercompaction of mitotic chromosomes in human cells.Nucleic acids research · 2014Article
- Direct monitoring of the strand passage reaction of DNA topoisomerase II triggers checkpoint activation.PLoS genetics · 2013Article
- Restoration of topoisomerase 2 function by complementation of defective monomers in Drosophila.Genetics · 2012Article
- Article
- Probing the differential interactions of quinazolinedione PD 0305970 and quinolones with gyrase and topoisomerase IV.Antimicrobial agents and chemotherapy · 2009Article
- Crystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigation.Nucleic acids research · 2009Article
- Isolation and characterization of mAMSA-hypersensitive mutants. Cytotoxicity of Top2 covalent complexes containing DNA single strand breaks.The Journal of biological chemistry · 2008Article
- The catalytically active tyrosine residues of both SPO11-1 and SPO11-2 are required for meiotic double-strand break induction in Arabidopsis.The Plant cell · 2007Article
- Meiotic association between Spo11 regulated by Rec102, Rec104 and Rec114.Nucleic acids research · 2007Article
- Experimental and computational investigations of Ser10 and Lys13 in the binding and cleavage of DNA substrates by Escherichia coli DNA topoisomerase I.Nucleic acids research · 2006Article
- Bacterial cell killing mediated by topoisomerase I DNA cleavage activity.The Journal of biological chemistry · 2005Article
- Importance of the fourth alpha-helix within the CAP homology domain of type II topoisomerase for DNA cleavage site recognition and quinolone action.Antimicrobial agents and chemotherapy · 2002Article
- Quinolone-binding pocket of DNA gyrase: role of GyrB.Antimicrobial agents and chemotherapy · 2002Article
- Involvement of conserved histidine, lysine and tyrosine residues in the mechanism of DNA cleavage by the caspase-3 activated DNase CAD.Nucleic acids research · 2002Article
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Authors and funding
2 authors.
Funding
Abstract
Studies of yeast DNA topoisomerase II with various alanine-substitution mutations provide strong biochemical support of a recent hypothesis that the type IA and IIA DNA topoisomerases act similarly in their cleavage and rejoining of DNA. DNA breakage and rejoining by either a type IA or a type IIA enzyme are shown to involve cooperation between a DNA-binding domain containing the active-site tyrosine and a Rossmann fold containing several highly conserved acidic residues. For a homodimeric type IIA enzyme, cooperation occurs in trans: the active-site tyrosine in the DNA-binding domain of one protomer cooperates with several residues in the Rossmann fold as well as other regions of the other protomer.
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