ReviewInternational journal of molecular sciences2018
Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase.
Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Microbial Natural Products Targeting theMicroorganisms · 2026Review
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- DNA Gyrase as a Target for Quinolones.Biomedicines · 2023Review
- What makes a type IIA topoisomerase a gyrase or a Topo IV?Nucleic acids research · 2021Review
- Consequences of producing DNA gyrase from a synthetic gyrBA operon in Salmonella enterica serovar Typhimurium.Molecular microbiology · 2021Article
- Towards Conformation-Sensitive Inhibition of Gyrase: Implications of Mechanistic Insight for the Identification and Improvement of Inhibitors.Molecules (Basel, Switzerland) · 2021Review
- Synthesis and Biological Evaluation of New Pyridothienopyrimidine Derivatives as Antibacterial Agents andAntibiotics (Basel, Switzerland) · 2020Article
- Antimicrobial Resistance Determinants Circulating among ThermophilicAntibiotics (Basel, Switzerland) · 2020Article
- Quinolone Complexes with Lanthanide Ions: An Insight into their Analytical Applications and Biological Activity.Molecules (Basel, Switzerland) · 2020Review
- Functional interactions between gyrase subunits are optimized in a species-specific manner.The Journal of biological chemistry · 2020Article
- Synthesis, Docking Studies, and In Vitro Evaluation of Some Novel Thienopyridines and Fused Thienopyridine-Quinolines as Antibacterial Agents and DNA Gyrase Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Closing the DNA replication cycle: from simple circular molecules to supercoiled and knotted DNA catenanes.Nucleic acids research · 2019Review
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gyrase is a type IIA topoisomerase that catalyzes negative supercoiling of DNA. The enzyme consists of two GyrA and two GyrB subunits. It is believed to introduce negative supercoils into DNA by converting a positive DNA node into a negative node through strand passage: First, it cleaves both DNA strands of a double-stranded DNA, termed the G-segment, and then it passes a second segment of the same DNA molecule, termed the T-segment, through the gap created. As a two-fold symmetric enzyme, gyrase contains two copies of all elements that are key for the supercoiling reaction: The GyrB subunits provide two active sites for ATP binding and hydrolysis. The GyrA subunits contain two C-terminal domains (CTDs) for DNA binding and wrapping to stabilize the positive DNA node, and two catalytic tyrosines for DNA cleavage. While the presence of two catalytic tyrosines has been ascribed to the necessity of cleaving both strands of the G-segment to enable strand passage, the role of the two ATP hydrolysis events and of the two CTDs has been less clear. This review summarizes recent results on the role of these duplicate elements for individual steps of the supercoiling reaction, and discusses the implications for the mechanism of DNA supercoiling.
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