ArticleNature communications2025
Functional interplay between condensin I and topoisomerase Iiα in single-molecule DNA compaction.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Dual phosphoregulatory mechanisms of condensin I revealed by biochemical reconstitution.PNAS nexus · 2026Article
- Histone Density and Dynamics Shape Mitotic Chromatid Architecture in Xenopus Egg Extracts.Genes to cells : devoted to molecular & cellular mechanisms · 2026Article
- Motorized chromosome models of mitotic chromosome folding.Nature communications · 2025Article
- Mitotic genome folding.The Journal of cell biology · 2025Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
Abstract
Condensin I and topoisomerase IIα (topo IIα) are chromosomal ATPases essential for mitotic chromosome assembly. Mechanistically how the two ATPases cooperate to assemble mitotic chromosomes remains unknown. Here we investigate the interplay between condensin I and topo IIα at single-molecule resolution. While condensin I alone exhibits ATP-dependent DNA loop formation, it generates stable, compact structures ("lumps") in the presence of topo IIα in a manner dependent on its C-terminal domain. These lumps predominantly contain a single condensin I complex and a single topo IIα dimer. The strand passage activity of topo IIα introduces DNA knots within the lumps, rendering them resistant to protease treatment. An ATP hydrolysis-deficient mutant of condensin I forms smaller lumps, in which the probability of DNA knotting is markedly reduced. Our findings demonstrate that topo IIα-mediated strand passage is functionally coupled with condensin I-mediated loop extrusion, providing insights into the mechanism underlying mitotic chromosome assembly.
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