Document Type
Article
Journal Title
International Journal of Molecular Sciences
Publication Date
2024
Volume
26
Abstract
In eukaryotic nuclei, DNA is wrapped around an octamer of core histones to form nucleosomes. H1 binds to the linker DNA of nucleosome to form the chromatosome, the next structural unit of chromatin. Structural features on individual chromatosomes contribute to chromatin structure, but not fully characterized. In addition to canonical nucleosomes composed of two copies each of histones H2A, H2B, H3, and H4 (H3 nucleosomes), centromeres chromatin contain nucleosomes in which H3 is replaced with its analog CENP-A, changing structural properties of CENP-A nucleosomes. Nothing is known about the interaction of H1 with CENP-A nucleosomes. Here we filled this gap and characterized the interaction of H1 histone with both types of nucleosomes. H1 does bind both types of the nucleosomes forming more compact chromosome particles with elevated affinity to H3 nucleosomes. H1 binding significantly increases the stability of chromatosomes preventing their spontaneous dissociation. In addition to binding to the entry-exit position of the DNA arms identified earlier, H1 is capable of bridging of distant DNA segments. H1 binding leads to the assembly of mononucleosomes in aggregates, stabilized by internucleosome interactions as well as bridging of the DNA arms of chromatosomes. Contribution of these finding to the chromatin structure and functions are discussed.
MeSH Headings
Nucleosomes, Histones, DNA, Protein Binding, Humans, Animals, Chromatin, Centromere Protein A
DOI Link
ISSN
1422-0067
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Rafa, Ahmed Yesvi; Filliaux, Shaun; and Lyubchenko, Yuri L., "Nanoscale Characterization of Interaction of Nucleosomes with H1 Linker Histone" (2024). Journal Articles: Pharmaceutical Sciences. 48.
https://digitalcommons.unmc.edu/cop_pharmsci_articles/48

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