ReviewNucleic acids research2011
The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks.
Review in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
50 citing papers in PubMed, 82 citations in OpenAlex.
- Quinoline-Based Scaffolds in Anticancer Drug Discovery: Molecular Targets, Synthetic Strategies, and Biological Advances.ChemMedChem · 2026Review
- Type II topoisomerase substrate geometry revealed through combined experiment and computation.bioRxiv : the preprint server for biology · 2026Article
- Deletion of TOP2B promoter using CRISPR-Cas9 induces senescence in HEK 293T cells.Biochemistry and biophysics reports · 2026Article
- DNA deformability in sequence-dependent capture of E. coli gyrase.Nature communications · 2026Article
- Supercoiled DNA recognition and cleavage control in topoisomerase VI.Nature communications · 2026Article
- Spo11: from topoisomerase VI to meiotic recombination initiator.Biochemical Society transactions · 2025Review
- Expression, Purification, and Measurement of DNA Supercoil Relaxation Activity by Eukaryotic Topoisomerase II.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural and functional insights into the T-even type bacteriophage topoisomerase II.Nature communications · 2024Article
- Defective Homologous Recombination Repair By Up-Regulating Lnc-HZ10/Ahr Loop in Human Trophoblast Cells Induced Miscarriage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Using energy to go downhill-a genoprotective role for ATPase activity in DNA topoisomerase II.Nucleic acids research · 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
- Etoposide promotes DNA loop trapping and barrier formation by topoisomerase II.Nature chemical biology · 2023Article
- Molecular mechanism of topoisomerase poisoning by the peptide antibiotic albicidin.Nature catalysis · 2023Article
- Unveiling the interdomain dynamics of type II DNA topoisomerase through all-atom simulations: Implications for understanding its catalytic cycle.Computational and structural biotechnology journal · 2023Article
- Catalytic Mechanism of ATP Hydrolysis in the ATPase Domain of Human DNA Topoisomerase IIα.Journal of chemical information and modeling · 2022Article
- DNA-Topology Simplification by Topoisomerases.Molecules (Basel, Switzerland) · 2021Review
- DNA topoisomerases: Advances in understanding of cellular roles and multi-protein complexes via structure-function analysis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Review
- Structural and functional characterization of the Spo11 core complex.Nature structural & molecular biology · 2021Article
- Expanding the type IIB DNA topoisomerase family: identification of new topoisomerase and topoisomerase-like proteins in mobile genetic elements.NAR genomics and bioinformatics · 2020Article
- Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Type II DNA topoisomerases (topos) catalyse changes in DNA topology by passing one double-stranded DNA segment through another. This reaction is essential to processes such as replication and transcription, but carries with it the inherent danger of permanent double-strand break (DSB) formation. All type II topos hydrolyse ATP during their reactions; however, only DNA gyrase is able to harness the free energy of hydrolysis to drive DNA supercoiling, an energetically unfavourable process. A long-standing puzzle has been to understand why the majority of type II enzymes consume ATP to support reactions that do not require a net energy input. While certain type II topos are known to 'simplify' distributions of DNA topoisomers below thermodynamic equilibrium levels, the energy required for this process is very low, suggesting that this behaviour is not the principal reason for ATP hydrolysis. Instead, we propose that the energy of ATP hydrolysis is needed to control the separation of protein-protein interfaces and prevent the accidental formation of potentially mutagenic or cytotoxic DSBs. This interpretation has parallels with the actions of a variety of molecular machines that catalyse the conformational rearrangement of biological macromolecules.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.