7K60

Cryo-EM structure of a chromatosome containing human linker histone H1.10

7K60 の概要

• エントリーDOI: 10.2210/pdb7k60/pdb
• 関連するPDBエントリー: 7K5X 7K5Y
• EMDBエントリー: 22685
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
• 機能のキーワード: chromatosome, nucleosome, linker histones, single-chain antibody, charge-charge interaction, chromatin, nuclear protein, nuclear protein-dna complex, nuclear protein/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 312751.27

構造登録者

Zhou, B.-R.,Bai, Y. (登録日: 2020-09-17, 公開日: 2020-11-25, 最終更新日: 2025-05-14)

主引用文献

Zhou, B.R.,Feng, H.,Kale, S.,Fox, T.,Khant, H.,de Val, N.,Ghirlando, R.,Panchenko, A.R.,Bai, Y.
Distinct Structures and Dynamics of Chromatosomes with Different Human Linker Histone Isoforms.
Mol.Cell, 81:166-182.e6, 2021

PubMed Abstract: The repeating structural unit of metazoan chromatin is the chromatosome, a nucleosome bound to a linker histone, H1. There are 11 human H1 isoforms with diverse cellular functions, but how they interact with the nucleosome remains elusive. Here, we determined the cryoelectron microscopy (cryo-EM) structures of chromatosomes containing 197 bp DNA and three different human H1 isoforms, respectively. The globular domains of all three H1 isoforms bound to the nucleosome dyad. However, the flanking/linker DNAs displayed substantial distinct dynamic conformations. Nuclear magnetic resonance (NMR) and H1 tail-swapping cryo-EM experiments revealed that the C-terminal tails of the H1 isoforms mainly controlled the flanking DNA orientations. We also observed partial ordering of the core histone H2A C-terminal and H3 N-terminal tails in the chromatosomes. Our results provide insights into the structures and dynamics of the chromatosomes and have implications for the structure and function of chromatin.

PubMed: 33238161
DOI: 10.1016/j.molcel.2020.10.038

実験手法

ELECTRON MICROSCOPY (3.12 Å)