7PFU

Nucleosome stack of the 4x207 nucleosome array containing H1

7PFU の概要

• エントリーDOI: 10.2210/pdb7pfu/pdb
• EMDBエントリー: 13380
• 分子名称: Histone H3.2, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total)
• 機能のキーワード: chromatin, nucleosomes, linker histone, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 783377.13

構造登録者

Dombrowski, M.,Cramer, P. (登録日: 2021-08-12, 公開日: 2022-08-03, 最終更新日: 2024-07-17)

主引用文献

Dombrowski, M.,Engeholm, M.,Dienemann, C.,Dodonova, S.,Cramer, P.
Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory.
Nat.Struct.Mol.Biol., 29:493-501, 2022

PubMed Abstract: Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions.

PubMed: 35581345
DOI: 10.1038/s41594-022-00768-w

実験手法

ELECTRON MICROSCOPY (5 Å)