ArticleThe Journal of biological chemistry2013
Chiral discrimination and writhe-dependent relaxation mechanism of human topoisomerase IIα.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 38 citations in OpenAlex.
- Networked salt-bridges mediate magnesium-dependent conformational dynamics and functional regulation in type IA topoisomerases.Nature communications · 2026Article
- MYC modulates TOP2A diffusion to promote substrate detection and activity.Nature communications · 2026Article
- Substrate accessibility regulation of human TopIIa decatenation by cohesin.Nature communications · 2025Article
- Human Topoisomerase IIα Promotes Chromatin Condensation Via a Phase Transition.bioRxiv : the preprint server for biology · 2024Article
- Chromatinization modulates topoisomerase II processivity.Nature communications · 2023Article
- Chromatinization Modulates Topoisomerase II Processivity.bioRxiv : the preprint server for biology · 2023Article
- Telling Your Right Hand from Your Left: The Effects of DNA Supercoil Handedness on the Actions of Type II Topoisomerases.International journal of molecular sciences · 2023Review
- Basis for the discrimination of supercoil handedness during DNA cleavage by human and bacterial type II topoisomerases.Nucleic acids research · 2023Article
- Etoposide promotes DNA loop trapping and barrier formation by topoisomerase II.Nature chemical biology · 2023Article
- Recognition of DNA Supercoil Handedness during Catenation Catalyzed by Type II Topoisomerases.Biochemistry · 2022Article
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- Two-Dimensional Gel Electrophoresis to Study the Activity of Type IIA Topoisomerases on Plasmid Replication Intermediates.Biology · 2021Article
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- Article
- The Impact of the C-Terminal Region on the Interaction of Topoisomerase II Alpha with Mitotic Chromatin.International journal of molecular sciences · 2019Article
- Kinetic pathways of topology simplification by Type-II topoisomerases in knotted supercoiled DNA.Nucleic acids research · 2019Article
- Activities of gyrase and topoisomerase IV on positively supercoiled DNA.Nucleic acids research · 2017Article
- Torque and buckling in stretched intertwined double-helix DNAs.Physical review. E · 2017Article
- 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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4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundHuman topoisomerase IIα unlinks catenated chromosomes and preferentially relaxes positive supercoils.
resultsSupercoil chirality, twist density, and tension determine topoisomerase IIα relaxation rate and processivity.
conclusionStrand passage rate is determined by the efficiency of transfer segment capture that is modulated by the topoisomerase C-terminal domains. SIGNIFICANCE: Single-molecule measurements reveal the mechanism of chiral discrimination and tension dependence of supercoil relaxation by human topoisomerase IIα. Type IIA topoisomerases (Topo IIA) are essential enzymes that relax DNA supercoils and remove links joining replicated chromosomes. Human topoisomerase IIα (htopo IIα), one of two human isoforms, preferentially relaxes positive supercoils, a feature shared with Escherichia coli topoisomerase IV (Topo IV). The mechanistic basis of this chiral discrimination remains unresolved. To address this important issue, we measured the relaxation of individual supercoiled and "braided" DNA molecules by htopo IIα using a magnetic tweezers-based single-molecule assay. Our study confirmed the chiral discrimination activity of htopo IIα and revealed that the strand passage rate depends on DNA twist, tension on the DNA, and the C-terminal domain (CTD). Similar to Topo IV, chiral discrimination by htopo IIα results from chiral interactions of the CTDs with DNA writhe. In contrast to Topo IV, however, these interactions lead to chiral differences in relaxation rate rather than processivity. Increasing tension or twist disrupts the CTD-DNA interactions with a subsequent loss of chiral discrimination. Together, these results suggest that transfer segment (T-segment) capture is the rate-limiting step in the strand passage cycle. We propose a model for T-segment capture that provides a mechanistic basis for chiral discrimination and provides a coherent explanation for the effects of DNA twist and tension on eukaryotic type IIA topoisomerases.
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