Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures
| Autor: | Xinfan Hua, Junhui Peng, Zhiyong Zhang, Chuang Yuan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
lcsh:QH426-470
Molecular dynamics Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences Histone variant H2A.B Histones 03 medical and health sciences chemistry.chemical_compound Genetics Nucleosome Humans Multiscale modeling Molecular Biology 030304 developmental biology Chromatin Fiber 0303 health sciences biology Protein Stability Research Linker DNA 0104 chemical sciences Chromatin Nucleosomes lcsh:Genetics Histone chemistry Coarse-grained simulations Chromatosome Mutation biology.protein Biophysics DNA Protein Binding |
| Zdroj: | Epigenetics & Chromatin Epigenetics & Chromatin, Vol 13, Iss 1, Pp 1-14 (2020) |
| ISSN: | 1756-8935 |
| Popis: | Background H2A.B, the most divergent histone variant of H2A, can significantly modulate nucleosome and chromatin structures. However, the related structural details and the underlying mechanism remain elusive to date. In this work, we built atomic models of the H2A.B-containing nucleosome core particle (NCP), chromatosome, and chromatin fiber. Multiscale modeling including all-atom molecular dynamics and coarse-grained simulations were then carried out for these systems. Results It is found that sequence differences at the C-terminal tail, the docking domain, and the L2 loop, between H2A.B and H2A are directly responsible for the DNA unwrapping in the H2A.B NCP, whereas the N-terminus of H2A.B may somewhat compensate for the aforementioned unwrapping effect. The assembly of the H2A.B NCP is more difficult than that of the H2A NCP. H2A.B may also modulate the interactions of H1 with both the NCP and the linker DNA and could further affect the higher-order structure of the chromatin fiber. Conclusions The results agree with the experimental results and may shed new light on the biological function of H2A.B. Multiscale modeling may be a valuable tool for investigating structure and dynamics of the nucleosome and the chromatin induced by various histone variants. |
| Databáze: | OpenAIRE |
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