Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant

Masaaki Sugiyama; Yasuhiro Arimura; Kazuyoshi Shirayama; Risa Fujita; Yojiro Oba; Nobuhiro Sato; Rintaro Inoue; Takashi Oda; Mamoru Sato; Richard K Heenan; Hitoshi Kurumizaka

doi:10.1016/j.bpj.2014.04.007

Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant

Biophys J. 2014 May 20;106(10):2206-13. doi: 10.1016/j.bpj.2014.04.007.

Authors

Affiliations

¹ Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan. Electronic address: [email protected].
² (‡)Laboratory of Structural Biology, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan.
³ Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
⁴ Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama 230-0045, Japan.
⁵ ISIS Facility, STFC Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK.
⁶ (‡)Laboratory of Structural Biology, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan. Electronic address: [email protected].

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Histones / chemistry*
Histones / metabolism*
Humans
Nucleosomes / metabolism*
Rotation

Substances

Histones
Nucleosomes