Contribution of histone N-terminal tails to the structure and stability of nucleosomes

被引:98
|
作者
Iwasaki, Wakana [1 ,2 ]
Miya, Yuta [1 ]
Horikoshi, Naoki [1 ]
Osakabe, Akihisa [1 ]
Taguchi, Hiroyuki [1 ]
Tachiwana, Hiroaki [1 ]
Shibata, Takehiko [2 ]
Kagawa, Wataru [1 ,3 ]
Kurumizaka, Hitoshi [1 ]
机构
[1] Waseda Univ, Grad Sch Adv Sci & Engn, Struct Biol Lab, Shinjuku Ku, Tokyo 1628480, Japan
[2] RIKEN, Wako, Saitama 3510198, Japan
[3] Meisei Univ, Sch Sci & Engn, Dept Interdisciplinary Sci & Engn, Program Chem & Life Sci, Hino, Tokyo 1918506, Japan
来源
FEBS OPEN BIO | 2013年 / 3卷
关键词
Histone tail; Nucleosome; Chromatin; Crystal structure; Thermal stability assay; CRYSTAL-STRUCTURE; CORE PARTICLE; AMINO TERMINI; H3; CHROMATIN; PROTEIN; H2B; DOMAINS; H4; ACCESSIBILITY;
D O I
10.1016/j.fob.2013.08.007
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
Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure. (C) 2013 The Authors. Published by Elsevier B.V. on behalf of Federation of European Biochemical Societies. All rights reserved.
引用
收藏
页码:363 / 369
页数:7
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