ArticleScientific reports2014
DNA G-segment bending is not the sole determinant of topology simplification by type II DNA topoisomerases.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Substrate accessibility regulation of human TopIIa decatenation by cohesin.Nature communications · 2025Article
- Extensive Bioinformatics Analyses Reveal a Phylogenetically Conserved Winged Helix (WH) Domain (Zτ) of Topoisomerase IIα, Elucidating Its Very High Affinity for Left-Handed Z-DNA and Suggesting Novel Putative Functions.International journal of molecular sciences · 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
- Article
- Condensin minimizes topoisomerase II-mediated entanglements of DNA in vivo.The EMBO journal · 2021Article
- A nucleotide resolution map of Top2-linked DNA breaks in the yeast and human genome.Nature communications · 2019Article
- Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.eLife · 2018Article
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
- The dynamic interplay between DNA topoisomerases and DNA topology.Biophysical reviews · 2016Review
- The Dynamic Interplay Between DNA Topoisomerases and DNA Topology.Biophysical reviews · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
DNA topoisomerases control the topology of DNA. Type II topoisomerases exhibit topology simplification, whereby products of their reactions are simplified beyond that expected based on thermodynamic equilibrium. The molecular basis for this process is unknown, although DNA bending has been implicated. To investigate the role of bending in topology simplification, the DNA bend angles of four enzymes of different types (IIA and IIB) were measured using atomic force microscopy (AFM). The enzymes tested were Escherichia coli topo IV and yeast topo II (type IIA enzymes that exhibit topology simplification), and Methanosarcina mazei topo VI and Sulfolobus shibatae topo VI (type IIB enzymes, which do not). Bend angles were measured using the manual tangent method from topographical AFM images taken with a novel amplitude-modulated imaging mode: small amplitude small set-point (SASS), which optimises resolution for a given AFM tip size and minimises tip convolution with the sample. This gave improved accuracy and reliability and revealed that all 4 topoisomerases bend DNA by a similar amount: ~120° between the DNA entering and exiting the enzyme complex. These data indicate that DNA bending alone is insufficient to explain topology simplification and that the 'exit gate' may be an important determinant of this process.
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