6FQ6

Class 2 : distorted nucleosome

6FQ6 の概要

• エントリーDOI: 10.2210/pdb6fq6/pdb
• EMDBエントリー: 4297 4298
• 分子名称: histone H3, Histone H4, Histone H2A, ... (6 entities in total)
• 機能のキーワード: nucleosome, cryo em, nucleosome sliding, chromatin remodeling, gene regulation
• 由来する生物種: Xenopus laevis; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 178714.38

構造登録者

Bilokapic, S.,Halic, M. (登録日: 2018-02-13, 公開日: 2018-04-18, 最終更新日: 2024-05-15)

主引用文献

Bilokapic, S.,Strauss, M.,Halic, M.
Structural rearrangements of the histone octamer translocate DNA.
Nat Commun, 9:1330-1330, 2018

PubMed Abstract: Nucleosomes, the basic unit of chromatin, package and regulate expression of eukaryotic genomes. Nucleosomes are highly dynamic and are remodeled with the help of ATP-dependent remodeling factors. Yet, the mechanism of DNA translocation around the histone octamer is poorly understood. In this study, we present several nucleosome structures showing histone proteins and DNA in different organizational states. We observe that the histone octamer undergoes conformational changes that distort the overall nucleosome structure. As such, rearrangements in the histone core α-helices and DNA induce strain that distorts and moves DNA at SHL 2. Distortion of the nucleosome structure detaches histone α-helices from the DNA, leading to their rearrangement and DNA translocation. Biochemical assays show that cross-linked histone octamers are immobilized on DNA, indicating that structural changes in the octamer move DNA. This intrinsic plasticity of the nucleosome is exploited by chromatin remodelers and might be used by other chromatin machineries.

PubMed: 29626188
DOI: 10.1038/s41467-018-03677-z

実験手法

ELECTRON MICROSCOPY (4 Å)