ArticleNucleic acids research2011
On the structure and dynamics of the complex of the nucleosome and the linker histone.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Epigenetics in development, disease, and therapy: from mechanisms to clinical interventions.Science China. Life sciences · 2026Review
- Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023Review
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
- Elucidating the influence of linker histone variants on chromatosome dynamics and energetics.Nucleic acids research · 2020Article
- Chromatin Compaction Multiscale Modeling: A Complex Synergy Between Theory, Simulation, and Experiment.Frontiers in molecular biosciences · 2020Review
- Sensitive effect of linker histone binding mode and subtype on chromatin condensation.Nucleic acids research · 2019Article
- Dynamic placement of the linker histone H1 associated with nucleosome arrangement and gene transcription in early Drosophila embryonic development.Cell death & disease · 2018Article
- Dependence of Chromatosome Structure on Linker Histone Sequence and Posttranslational Modification.Biophysical journal · 2018Article
- Emerging roles of linker histones in regulating chromatin structure and function.Nature reviews. Molecular cell biology · 2018Review
- Dependence of the Linker Histone and Chromatin Condensation on the Nucleosome Environment.The journal of physical chemistry. B · 2017Article
- The effect of epigenetic modifications on the secondary structures and possible binding positions of the N-terminal tail of histone H3 in the nucleosome: a computational study.Journal of molecular modeling · 2017Article
- Conformational selection and dynamic adaptation upon linker histone binding to the nucleosome.Nucleic acids research · 2016Article
- Coupling between Histone Conformations and DNA Geometry in Nucleosomes on a Microsecond Timescale: Atomistic Insights into Nucleosome Functions.Journal of molecular biology · 2016Article
- SDA 7: A modular and parallel implementation of the simulation of diffusional association software.Journal of computational chemistry · 2015Article
- webSDA: a web server to simulate macromolecular diffusional association.Nucleic acids research · 2015Article
- The chromatin fiber: multiscale problems and approaches.Current opinion in structural biology · 2015Review
- Nucleosome structure and function.Chemical reviews · 2015Review
- Dynamic condensation of linker histone C-terminal domain regulates chromatin structure.Nucleic acids research · 2014Article
- Regulation of the nucleosome repeat length in vivo by the DNA sequence, protein concentrations and long-range interactions.PLoS computational biology · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several different models of the linker histone (LH)-nucleosome complex have been proposed, but none of them has unambiguously revealed the position and binding sites of the LH on the nucleosome. Using Brownian dynamics-based docking together with normal mode analysis of the nucleosome to account for the flexibility of two flanking 10 bp long linker DNAs (L-DNA), we identified binding modes of the H5-LH globular domain (GH5) to the nucleosome. For a wide range of nucleosomal conformations with the L-DNA ends less than 65 Å apart, one dominant binding mode was identified for GH5 and found to be consistent with fluorescence recovery after photobleaching (FRAP) experiments. GH5 binds asymmetrically with respect to the nucleosomal dyad axis, fitting between the nucleosomal DNA and one of the L-DNAs. For greater distances between L-DNA ends, docking of GH5 to the L-DNA that is more restrained and less open becomes favored. These results suggest a selection mechanism by which GH5 preferentially binds one of the L-DNAs and thereby affects DNA dynamics and accessibility and contributes to formation of a particular chromatin fiber structure. The two binding modes identified would, respectively, favor a tight zigzag chromatin structure or a loose solenoid chromatin fiber.
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