ReviewNucleic acids research2021
What makes a type IIA topoisomerase a gyrase or a Topo IV?
Review in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 45 citations in OpenAlex.
- Novel Bacterial Topoisomerase Inhibitors: A New Front in an Old War.Journal of molecular biology · 2026Review
- Design, synthesis, and antibacterial efficacy of new methylene disalicylic acid/1,3,4-oxadiazole hybrids as dual inhibitors of DNA gyrase and topoisomerase IV.Molecular diversity · 2026Article
- A Review of Fluoroquinolones with a Focus on Veterinary-Approved Agents.Biomolecules · 2026Review
- A high-throughput fluorescent DNA cleavage assay for discovering bacterial DNA gyrase poisons.Nucleic acids research · 2026Article
- Bacterial type II topoisomerases cleave DNA in a species-specific manner.Nucleic acids research · 2026Article
- The Difluoroboranyl-Fluoroquinolone Derivative "7a" Inhibits Bacterial DNA Gyrase and Exhibits Potent Activity Against Ciprofloxacin-ResistantMolecules (Basel, Switzerland) · 2026Article
- Enzyme-DNA Interactions Affect the Catalytic Inhibition of Mycobacterial Gyrases by Antibacterial Drugs.ACS infectious diseases · 2026Article
- Direct trapping of the transport-segment DNA by the central domain of type IIA topoisomerases.Science advances · 2025Article
- Structural interactions of BWC0977 with Klebsiella pneumoniae topoisomerase IV and biochemical basis of its broad-spectrum activity.Communications biology · 2025Article
- Article
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- The Derivative Difluoroboranyl-Fluoroquinolone "7a" Generates Effective Inhibition Against theCurrent issues in molecular biology · 2025Article
- Hallmarks of DNA replication stress responses in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2025Review
- Optimal Effective Concentration Combinations and synergy evaluations for binary antimicrobial combinationsFrontiers in microbiology · 2025Article
- DNA Supercoiling Catalyzed by Bacterial Gyrase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural and functional insights into the T-even type bacteriophage topoisomerase II.Nature communications · 2024Article
- Review and Current Perspectives on DNA Topoisomerase I and II Enzymes of Fungi as Study Models for the Development of New Antifungal Drugs.Journal of fungi (Basel, Switzerland) · 2024Review
- Interactions between Zoliflodacin andACS infectious diseases · 2024Article
- Article
- Interactions between Gepotidacin andACS infectious diseases · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type IIA topoisomerases catalyze a variety of different reactions: eukaryotic topoisomerase II relaxes DNA in an ATP-dependent reaction, whereas the bacterial representatives gyrase and topoisomerase IV (Topo IV) preferentially introduce negative supercoils into DNA (gyrase) or decatenate DNA (Topo IV). Gyrase and Topo IV perform separate, dedicated tasks during replication: gyrase removes positive supercoils in front, Topo IV removes pre-catenanes behind the replication fork. Despite their well-separated cellular functions, gyrase and Topo IV have an overlapping activity spectrum: gyrase is also able to catalyze DNA decatenation, although less efficiently than Topo IV. The balance between supercoiling and decatenation activities is different for gyrases from different organisms. Both enzymes consist of a conserved topoisomerase core and structurally divergent C-terminal domains (CTDs). Deletion of the entire CTD, mutation of a conserved motif and even by just a single point mutation within the CTD converts gyrase into a Topo IV-like enzyme, implicating the CTDs as the major determinant for function. Here, we summarize the structural and mechanistic features that make a type IIA topoisomerase a gyrase or a Topo IV, and discuss the implications for type IIA topoisomerase evolution.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.