ArticleNucleic acids research2007
Topoisomerase II, scaffold component, promotes chromatin compaction in vitro in a linker-histone H1-dependent manner.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Spatial-Temporal Genome Regulation in Stress-Response and Cell-Fate Change.International journal of molecular sciences · 2023Review
- Viral origin of eukaryotic type IIA DNA topoisomerases.Virus evolution · 2022Article
- Single-Molecule/Cell Analyses Reveal Principles of Genome-Folding Mechanisms in the Three Domains of Life.International journal of molecular sciences · 2021Review
- Comparing Super-Resolution Microscopy Techniques to Analyze Chromosomes.International journal of molecular sciences · 2021Article
- Different Proteins Mediate Step-Wise Chromosome Architectures inFrontiers in microbiology · 2020Article
- Volume Transitions of Isolated Cell Nuclei Induced by Rapid Temperature Increase.Biophysical journal · 2017Article
- Physiological Roles of DNA Double-Strand Breaks.Journal of nucleic acids · 2017Review
- Lamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation.The Journal of biological chemistry · 2012Article
- Local sensing of global DNA topology: from crossover geometry to type II topoisomerase processivity.Nucleic acids research · 2011Article
- Nuclear architecture and chromatin dynamics revealed by atomic force microscopy in combination with biochemistry and cell biology.Pflugers Archiv : European journal of physiology · 2008Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TopoisomeraseII (Topo II) is a major component of chromosomal scaffolds and essential for mitotic chromosome condensation, but the mechanism of this action remains unknown. Here, we used an in vitro chromatin reconstitution system in combination with atomic force and fluorescence microscopic analyses to determine how Topo II affects chromosomal structure. Topo II bound to bare DNA and clamped the two DNA strands together, even in the absence of ATP. In addition, Topo II promoted chromatin compaction in a manner dependent on histone H1 but independent of ATP. Histone H1-induced 30-nm chromatin fibers were converted into a large complex by Topo II. Fluorescence microscopic analysis of the Brownian motion of chromatin stained with 4',6-diamidino-2-phenylindole showed that the reconstituted chromatin became larger following the addition of Topo II in the presence but not the absence of histone H1. Based on these findings, we propose that chromatin packing is triggered by histone H1-dependent, Topo II-mediated clamping of DNA strands.
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