共 55 条
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
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Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Murphy, Kevin J.
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Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Kujirai, Tomoya
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机构:
Univ Tokyo, Inst Quantitat Biosci, Lab Chromatin Struct & Funct, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1130032, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

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Kato, Junko
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Univ Tokyo, Inst Quantitat Biosci, Lab Chromatin Struct & Funct, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1130032, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Koyama, Masako
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Univ Tokyo, Inst Quantitat Biosci, Lab Chromatin Struct & Funct, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1130032, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Okamato, Akimitsu
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机构:
Univ Tokyo, Grad Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, 7-3-1 Hongo, Tokyo 1138656, Japan
Univ Tokyo, Res Ctr Adv Sci & Technol, Meguro Ku, 4-6-1 Komaba, Tokyo 1538904, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Hayashi, Gosuke
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机构:
Nagoya Univ, Grad Sch Engn, Dept Biomol Engn, Chikusa Ku, Nagoya, Aichi 4648603, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Kurumizaka, Hitoshi
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机构:
Univ Tokyo, Inst Quantitat Biosci, Lab Chromatin Struct & Funct, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1130032, Japan Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA

Hayes, Jeffrey J.
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h-index: 0
机构:
Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14642 USA
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.
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收藏
页码:11510 / 11520
页数:11
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