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

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2206-2213
Number of pages	8
Journal	Biophysical Journal
Volume	106
Issue number	10
DOIs	https://doi.org/10.1016/j.bpj.2014.04.007
Publication status	Published - 2014 May 20

ASJC Scopus subject areas

Biophysics
Medicine(all)

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10.1016/j.bpj.2014.04.007

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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.",

author = "Masaaki Sugiyama and Yasuhiro Arimura and Kazuyoshi Shirayama and Risa Fujita and Yojiro Oba and Nobuhiro Sato and Rintaro Inoue and Takashi Oda and Mamoru Sato and Heenan, {Richard K.} and Hitoshi Kurumizaka",

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T1 - Distinct features of the histone core structure in nucleosomes containing the histone h2a.b variant

AU - Sugiyama, Masaaki

AU - Arimura, Yasuhiro

AU - Shirayama, Kazuyoshi

AU - Fujita, Risa

AU - Oba, Yojiro

AU - Sato, Nobuhiro

AU - Inoue, Rintaro

AU - Oda, Takashi

AU - Sato, Mamoru

AU - Heenan, Richard K.

AU - Kurumizaka, Hitoshi

PY - 2014/5/20

Y1 - 2014/5/20

N2 - 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.

AB - 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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Distinct features of the histone core structure in nucleosomes containing the histone h2a.b variant

Abstract

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