ArticleBiophysical journal2014
Characterization of nucleosome unwrapping within chromatin fibers using magnetic tweezers.
Article in Biophysical journal, 2014. 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, 28 citations in OpenAlex.
- Multiscale Architecture and Mechanics of the Cell Nucleus: Implications for Disease, Bioengineering and Nanomedicine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Insights from single-molecule force spectroscopy into chromatin topology.Biophysical reviews · 2026Review
- Beyond the mono-nucleosome.Biochemical Society transactions · 2025Review
- Dynamics of nucleosomes and chromatin fibers revealed by single-molecule measurements.BMB reports · 2025Review
- A Molecular View into the Structure and Dynamics of Phase-Separated Chromatin.The journal of physical chemistry. B · 2024Article
- Cisplatin fastens chromatin irreversibly even at a high chloride concentration.Nucleic acids research · 2021Article
- Nucleosome plasticity is a critical element of chromatin liquid-liquid phase separation and multivalent nucleosome interactions.Nature communications · 2021Article
- Torsional stress can regulate the unwrapping of two outer half superhelical turns of nucleosomal DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability.Nature communications · 2020Article
- Multiplexed Nanometric 3D Tracking of Microbeads Using an FFT-Phasor Algorithm.Biophysical journal · 2020Article
- Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019Review
- Dynamics of Chromatin Fibers: Comparison of Monte Carlo Simulations with Force Spectroscopy.Biophysical journal · 2018Article
- Free energy profiles for unwrapping the outer superhelical turn of nucleosomal DNA.PLoS computational biology · 2018Article
- Nucleosome stability measured in situ by automated quantitative imaging.Scientific reports · 2017Article
- Electrostatic forces govern the binding mechanism of intrinsically disordered histone chaperones.PloS one · 2017Article
- Uncovering the forces between nucleosomes using DNA origami.Science advances · 2016Article
- The chromatin fiber: multiscale problems and approaches.Current opinion in structural biology · 2015Review
- Data on force-dependent structural changes of chromatin fibers measured with magnetic tweezers.Data in brief · 2014Article
Corrections and comments
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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
Nucleosomal arrays fold into chromatin fibers and the higher-order folding of chromatin plays a strong regulatory role in all processes involving DNA access, such as transcription and replication. A fundamental understanding of such regulation requires insight into the folding properties of the chromatin fiber in molecular detail. Despite this, the structure and the mechanics of chromatin fibers remain highly disputed. Single-molecule force spectroscopy experiments have the potential to provide such insight, but interpretation of the data has been hampered by the large variations in experimental force-extension traces. Here we explore the possibility that chromatin fibers are composed of both single-turn and fully wrapped histone octamers. By characterizing the force-dependent behavior of in vitro reconstituted chromatin fibers and reanalyzing existing data, we show the unwrapping of the outer turn of nucleosomal DNA at 3 pN. We present a model composed of two freely-jointed chains, which reveals that nucleosomes within the chromatin fiber show identical force-extension behavior to mononucleosomes, indicating that nucleosome-nucleosome interactions are orders-of-magnitude smaller than previously reported and therefore can be overcome by thermal fluctuations. We demonstrate that lowering the salt concentration externally increases the wrapping energy significantly, indicative of the electrostatic interaction between the wrapped DNA and the histone octamer surface. We propose that the weak interaction between nucleosomes could allow easy access to nucleosomal DNA, while DNA unwrapping from the histone core could provide a stable yet dynamic structure during DNA maintenance.
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