ArticlePloS one2008
The impact of the human DNA topoisomerase II C-terminal domain on activity.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- 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
- Modeling allosteric mechanisms of eukaryotic type II topoisomerases.Biophysical journal · 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
- 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
- Article
- Mutations in topoisomerase IIβ result in a B cell immunodeficiency.Nature communications · 2019Article
- The Impact of the C-Terminal Region on the Interaction of Topoisomerase II Alpha with Mitotic Chromatin.International journal of molecular sciences · 2019Article
- 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
- Roles of the C-terminal domains of topoisomerase IIα and topoisomerase IIβ in regulation of the decatenation checkpoint.Nucleic acids research · 2017Article
- Physiological Roles of DNA Double-Strand Breaks.Journal of nucleic acids · 2017Review
- Topoisomerase II from Human Malaria Parasites: EXPRESSION, PURIFICATION, AND SELECTIVE INHIBITION.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
backgroundType II DNA topoisomerases (topos) are essential enzymes needed for the resolution of topological problems that occur during DNA metabolic processes. Topos carry out an ATP-dependent strand passage reaction whereby one double helix is passed through a transient break in another. Humans have two topoII isoforms, alpha and beta, which while enzymatically similar are differentially expressed and regulated, and are thought to have different cellular roles. The C-terminal domain (CTD) of the enzyme has the most diversity, and has been implicated in regulation. We sought to investigate the impact of the CTD domain on activity. METHODOLOGY/PRINCIPLE
findingsWe have investigated the role of the human topoII C-terminal domain by creating constructs encoding C-terminally truncated recombinant topoIIalpha and beta and topoIIalpha+beta-tail and topoIIbeta+alpha-tail chimeric proteins. We then investigated function in vivo in a yeast system, and in vitro in activity assays. We find that the C-terminal domain of human topoII isoforms is needed for in vivo function of the enzyme, but not needed for cleavage activity. C-terminally truncated enzymes had similar strand passage activity to full length enzymes, but the presence of the opposite C-terminal domain had a large effect, with the topoIIalpha-CTD increasing activity, and the topoIIbeta-CTD decreasing activity. CONCLUSIONS/SIGNIFICANCE: In vivo complementation data show that the topoIIalpha C-terminal domain is needed for growth, but the topoIIbeta isoform is able to support low levels of growth without a C-terminal domain. This may indicate that topoIIbeta has an additional localisation signal. In vitro data suggest that, while the lack of any C-terminal domain has little effect on activity, the presence of either the topoIIalpha or beta C-terminal domain can affect strand passage activity. Data indicates that the topoIIbeta-CTD may be a negative regulator. This is the first report of in vitro data with chimeric human topoIIs.
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