ArticlePloS one2011
The impact of the C-terminal domain on the interaction of human DNA topoisomerase II α and β with DNA.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- The Roles of Topoisomerases in Transcriptional Regulation.International journal of molecular sciences · 2026Review
- Mutagenesis of Intrinsically Disordered Domain Impacts Topoisomerase IIα Catalytic Activity.International journal of molecular sciences · 2025Article
- Human Topoisomerase IIα Promotes Chromatin Condensation Via a Phase Transition.bioRxiv : the preprint server for biology · 2024Article
- Bioinformatic Analysis of Topoisomerase IIα Reveals Interdomain Interdependencies and Critical C-Terminal Domain Residues.International journal of molecular sciences · 2024Article
- MeCP2 represses the activity of topoisomerase IIβ in long neuronal genes.Cell reports · 2023Article
- Methylated histones on mitotic chromosomes promote topoisomerase IIα function for high fidelity chromosome segregation.iScience · 2023Article
- Untangling the roles of TOP2A and TOP2B in transcription and cancer.Science advances · 2022Review
- Calcineurin dephosphorylates topoisomerase IIβ and regulates the formation of neuronal-activity-induced DNA breaks.Molecular cell · 2022Article
- Topoisomerase VI participates in an insulator-like function that prevents H3K9me2 spreading.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Exploration of the Role of the C-Terminal Domain of Human DNA Topoisomerase IIα in Catalytic Activity.ACS omega · 2021Article
- Structural basis for allosteric regulation of Human Topoisomerase IIα.Nature communications · 2021Article
- Histone H2A phosphorylation recruits topoisomerase IIα to centromeres to safeguard genomic stability.The EMBO journal · 2020Article
- TOP2B: The First Thirty Years.International journal of molecular sciences · 2018Review
- The Roles of DNA Topoisomerase IIβ in Transcription.International journal of molecular sciences · 2018Review
- Non-Catalytic Roles of the Topoisomerase IIα C-Terminal Domain.International journal of molecular sciences · 2017Review
- Fluoroquinolones stimulate the DNA cleavage activity of topoisomerase IV by promoting the binding of Mg(2+) to the second metal binding site.Biochimica et biophysica acta · 2016Article
- Nuclear dynamics of topoisomerase IIβ reflects its catalytic activity that is regulated by binding of RNA to the C-terminal domain.Nucleic acids research · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundType II DNA topoisomerases are essential, ubiquitous enzymes that act to relieve topological problems arising in DNA from normal cellular activity. Their mechanism of action involves the ATP-dependent transport of one DNA duplex through a transient break in a second DNA duplex; metal ions are essential for strand passage. Humans have two isoforms, topoisomerase IIα and topoisomerase IIβ, that have distinct roles in the cell. The C-terminal domain has been linked to isoform specific differences in activity and DNA interaction. METHODOLOGY/PRINCIPAL
findingsWe have investigated the role of the C-terminal domain in the binding of human topoisomerase IIα and topoisomerase IIβ to DNA in fluorescence anisotropy assays using full length and C-terminally truncated enzymes. We find that the C-terminal domain of topoisomerase IIβ but not topoisomerase IIα affects the binding of the enzyme to the DNA. The presence of metal ions has no effect on DNA binding. Additionally, we have examined strand passage of the full length and truncated enzymes in the presence of a number of supporting metal ions and find that there is no difference in relative decatenation between isoforms. We find that calcium and manganese, in addition to magnesium, can support strand passage by the human topoisomerase II enzymes. CONCLUSIONS/SIGNIFICANCE: The C-terminal domain of topoisomerase IIβ, but not that of topoisomerase IIα, alters the enzyme's K(D) for DNA binding. This is consistent with previous data and may be related to the differential modes of action of the two isoforms in vivo. We also show strand passage with different supporting metal ions for human topoisomerase IIα or topoisomerase IIβ, either full length or C-terminally truncated. They all show the same preferences, whereby Mg > Ca > Mn.
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