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Updated: Apr 29, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
Published on: September 10, 2013
Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant
Masaaki Sugiyama1, Yasuhiro Arimura2, Kazuyoshi Shirayama2
1Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
Abstract:
Nucleosomes containing a human histone variant, H2A.B, in an aqueous solution were analyzed by small-angle neutron scattering utilizing a contrast variation technique. Comparisons with the canonical H2A nucleosome structure revealed that the DNA termini of the H2A.B nucleosome are detached from the histone core surface, and flexibly expanded toward the solvent. In contrast, the histone tails are compacted in H2A.B nucleosomes compared to those in canonical H2A nucleosomes, suggesting that they bind to the surface of the histone core and/or DNA. Therefore, the histone tail dynamics may function to regulate the flexibility of the DNA termini in the nucleosomes.
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