Structure and function of human histone H3.Y nucleosome

被引：41

作者：

Kujirai, Tomoya ^{[1
]}

Horikoshi, Naoki ^{[2
]}

Sato, Koichi ^{[1
]}

Maehara, Kazumitsu ^{[3
]}

Machida, Shinichi ^{[1
]}

Osakabe, Akihisa ^{[1
]}

Kimura, Hiroshi ^{[4
]}

Ohkawa, Yasuyuki ^{[3
]}

Kurumizaka, Hitoshi ^{[1
,2
,5
]}

机构：

[1] Waseda Univ, Grad Sch Adv Sci & Engn, Struct Biol Lab, Shinjuku Ku, 2-2 Wakamatsu Cho, Tokyo 1628480, Japan

[2] Waseda Univ, Res Inst Sci & Engn, Shinjuku Ku, 2-2 Wakamatsu Cho, Tokyo 1628480, Japan

[3] Kyushu Univ, Med Inst Bioregulat, Div Transcript, Higashi Ku, 3-1-1 Maidashi, Fukuoka 8128582, Japan

[4] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Biol Sci, Yokohama, Kanagawa 2268501, Japan

[5] Waseda Univ, Inst Med Oriented Struct Biol, Shinjuku Ku, 2-2 Wakamatsu Cho, Tokyo 1628480, Japan

来源：

NUCLEIC ACIDS RESEARCH | 2016年 / 44卷 / 13期

基金：

日本学术振兴会;

关键词：

CRYSTAL-STRUCTURE; CENP-A; CORE PARTICLES; CHROMATIN; VARIANTS; EXPRESSION; STABILITY; CHAPERONE; LANGUAGE; DYNAMICS;

D O I：

10.1093/nar/gkw202

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Histone H3.Y is a primate-specific, distant H3 variant. It is evolutionarily derived from H3.3, and may function in transcription regulation. However, the mechanism by which H3.Y regulates transcription has not been elucidated. In the present study, we determined the crystal structure of the H3. Y nucleosome, and found that many H3.Y-specific residues are located on the entry/exit sites of the nucleosome. Biochemical analyses revealed that the DNA ends of the H3.Y nucleosome were more flexible than those of the H3.3 nucleosome, although the H3. Y nucleosome was stable in vitro and in vivo. Interestingly, the linker histone H1, which compacts nucleosomal DNA, appears to bind to the H3. Y nucleosome less efficiently, as compared to the H3.3 nucleosome. These characteristics of the H3. Y nucleosome are also conserved in the H3. Y/H3.3 heterotypic nucleosome, which may be the predominant form in cells. In human cells, H3. Y preferentially accumulated around transcription start sites (TSSs). Taken together, H3.Y-containing nucleosomes around transcription start sites may form relaxed chromatin that allows transcription factor access, to regulate the transcription status of specific genes.

引用

页码：6127 / 6141

页数：15

共 65 条

[1] PHENIX: a comprehensive Python']Python-based system for macromolecular structure solution [J].