ArticleNucleic acids research2007
DNA topoisomerase II selects DNA cleavage sites based on reactivity rather than binding affinity.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- G-quadruplex structures as regulators of cellular processes and drivers of genome instability in cancer.Critical reviews in biochemistry and molecular biology · 2026Review
- Synthesis of azole-linkedNanoscale advances · 2026Article
- Complex mechanisms of topoisomerase II poisons revealed by whole-genome analysis.Communications biology · 2026Article
- Highly sensitive mapping of in vitro type II topoisomerase DNA cleavage sites with SHAN-seq.Nucleic acids research · 2024Article
- Highly sensitive mapping ofbioRxiv : the preprint server for biology · 2024Article
- Novel topoisomerase II/EGFR dual inhibitors: design, synthesis and docking studies of naphtho[2',3':4,5]thiazolo[3,2-Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Recurrent mutations in topoisomerase IIα cause a previously undescribed mutator phenotype in human cancers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion.Journal of molecular biology · 2019Review
- Selection of DNA Cleavage Sites by Topoisomerase II Results from Enzyme-Induced Flexibility of DNA.Cell chemical biology · 2019Article
- Genome-wide TOP2A DNA cleavage is biased toward translocated and highly transcribed loci.Genome research · 2017Article
- DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism.Nucleic acids research · 2016Article
- E. coli Gyrase Fails to Negatively Supercoil Diaminopurine-Substituted DNA.Journal of molecular biology · 2015Article
- Distinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.Journal of molecular biology · 2013Article
- The role of DNA bending in type IIA topoisomerase function.Nucleic acids research · 2013Article
- Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity.Nature structural & molecular biology · 2012Article
- DNA cleavage and opening reactions of human topoisomerase IIα are regulated via Mg2+-mediated dynamic bending of gate-DNA.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The DNA binding CXC domain of MSL2 is required for faithful targeting the Dosage Compensation Complex to the X chromosome.Nucleic acids research · 2010Article
- The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The why and how of DNA unlinking.Nucleic acids research · 2009Review
- Coupling between ATP binding and DNA cleavage by DNA topoisomerase II: A unifying kinetic and structural mechanism.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
DNA topoisomerase II modulates DNA topology by relieving supercoil stress and by unknotting or decatenating entangled DNA. During its reaction cycle, the enzyme creates a transient double-strand break in one DNA segment, the G-DNA. This break serves as a gate through which another DNA segment is transported. Defined topoisomerase II cleavage sites in genomic and plasmid DNA have been previously mapped. To dissect the G-DNA recognition mechanism, we studied the affinity and reactivity of a series of DNA duplexes of varied sequence under conditions that only allow G-DNA to bind. These DNA duplexes could be cleaved to varying extents ranging from undetectable (<0.5%) to 80%. The sequence that defines a cleavage site resides within the central 20 bp of the duplex. The DNA affinity does not correlate with the ability of the enzyme to cleave DNA, suggesting that the binding step does not contribute significantly to the selection mechanism. Kinetic experiments show that the selectivity interactions are formed before rather than subsequent to cleavage. Presumably the binding energy of the cognate interactions is used to promote a conformational change that brings the enzyme into a cleavage competent state. The ability to modulate the extent of DNA cleavage by varying the DNA sequence may be valuable for future structural and mechanistic studies that aim to determine topoisomerase structures with DNA bound in pre- and post-cleavage states and to understand the conformational changes associated with DNA binding and cleavage.
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