ArticlePloS one2017
Atomic force microscopy of chromatin arrays reveal non-monotonic salt dependence of array compaction in solution.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Analysis of DNA-Protein Complexes by Atomic Force Microscopy Imaging: The Case of TRF2-Telomeric DNA Wrapping.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Article
- Histone variant H2BE enhances chromatin accessibility in neurons to promote synaptic gene expression and long-term memory.Molecular cell · 2024Article
- A nucleosome switch primes Hepatitis B Virus infection.bioRxiv : the preprint server for biology · 2024Article
- Histone variant H2BE enhances chromatin accessibility in neurons to promote synaptic gene expression and long-term memory.bioRxiv : the preprint server for biology · 2024Article
- Atomic Force Microscopy Characterization of Reconstituted Protein-DNA Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- DNA-binding proteins studied by mechanical manipulation and AFM imaging of single DNA molecules.Biophysics reports · 2022Article
- Bending and looping of long DNA by Polycomb repressive complex 2 revealed by AFM imaging in liquid.Nucleic acids research · 2020Article
- Chromatin Compaction Multiscale Modeling: A Complex Synergy Between Theory, Simulation, and Experiment.Frontiers in molecular biosciences · 2020Review
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
Compaction of DNA in chromatin is a hallmark of the eukaryotic cell and unravelling its structure is required for an understanding of DNA involving processes. Despite strong experimental efforts, many questions concerning the DNA packing are open. In particular, it is heavily debated whether an ordered structure referred to as the "30 nm fibre" exist in vivo. Scanning probe microscopy has become a cutting edge technology for the high-resolution imaging of DNA- protein complexes. Here, we perform high-resolution atomic force microscopy of non-cross-linked chromatin arrays in liquid, under different salt conditions. A statistical analysis of the data reveals that array compaction is salt dependent in a non-monotonic fashion. A simple physical model can qualitatively explain the observed findings due to the opposing effects of salt dependent stiffening of DNA, nucleosome stability and histone-histone interactions. While for different salt concentrations different compaction states are observed, our data do not provide support for the existence of regular chromatin fibres. Our studies add new insights into chromatin structure, and with that contribute to a further understanding of the DNA condensation.
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