Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain

被引:12
作者
Hao, Fanfan [1 ]
Murphy, Kevin J. [1 ]
Kujirai, Tomoya [2 ]
Kamo, Naoki [3 ]
Kato, Junko [2 ]
Koyama, Masako [2 ]
Okamato, Akimitsu [3 ,4 ]
Hayashi, Gosuke [5 ]
Kurumizaka, Hitoshi [2 ]
Hayes, Jeffrey J. [1 ]
机构
[1] Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA
[2] Univ Tokyo, Inst Quantitat Biosci, Lab Chromatin Struct & Funct, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1130032, Japan
[3] Univ Tokyo, Grad Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, 7-3-1 Hongo, Tokyo 1138656, Japan
[4] Univ Tokyo, Res Ctr Adv Sci & Technol, Meguro Ku, 4-6-1 Komaba, Tokyo 1538904, Japan
[5] Nagoya Univ, Grad Sch Engn, Dept Biomol Engn, Chikusa Ku, Nagoya, Aichi 4648603, Japan
基金
美国国家卫生研究院;
关键词
AMINO-ACID-COMPOSITION; HISTONE H1; CHROMATIN-STRUCTURE; LINKER DNA; SECONDARY STRUCTURE; NUCLEOSOMAL ARRAYS; CORE; PROTEIN; DYNAMICS; BINDING;
D O I
10.1093/nar/gkaa949
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
Linker histones (H1s) are key structural components of the chromatin of higher eukaryotes. However, the mechanisms by which the intrinsically disordered linker histone carboxy-terminal domain (H1 CTD) influences chromatin structure and gene regulation remain unclear. We previously demonstrated that the CTD of H1.0 undergoes a significant condensation (reduction of end-to-end distance) upon binding to nucleosomes, consistent with a transition to an ordered structure or ensemble of structures. Here, we show that deletion of the H3 N-terminal tail or the installation of acetylation mimics or bona fide acetylation within H3 N-terminal tail alters the condensation of the nucleosome-bound H1 CTD. Additionally, we present evidence that the H3 N-tail influences H1 CTD condensation through direct protein-protein interaction, rather than alterations in linker DNA trajectory. These results support an emerging hypothesis wherein the H1 CTD serves as a nexus for signaling in the nucleosome.
引用
收藏
页码:11510 / 11520
页数:11
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