9GD2

Structure of Chd1 bound to a dinucleosome with a dyad-to-dyad distance of 103 bp.

これはPDB形式変換不可エントリーです。

9GD2 の概要

• エントリーDOI: 10.2210/pdb9gd2/pdb
• EMDBエントリー: 51244
• 分子名称: Histone H3.2, MAGNESIUM ION, Histone H4, ... (10 entities in total)
• 機能のキーワード: chromatin, remodeling, transcription, nucleosome, dna binding protein
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 877549.47

構造登録者

Engeholm, M.,Roske, J.J.,Oberbeckmann, E.,Dienemann, C.,Lidschreiber, M.,Cramer, P.,Farnung, L. (登録日: 2024-08-04, 公開日: 2024-09-18, 最終更新日: 2024-10-02)

主引用文献

Engeholm, M.,Roske, J.J.,Oberbeckmann, E.,Dienemann, C.,Lidschreiber, M.,Cramer, P.,Farnung, L.
Resolution of transcription-induced hexasome-nucleosome complexes by Chd1 and FACT.
Mol.Cell, 84:3423-, 2024

PubMed Abstract: To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase II (RNAPII) generates hexasomes that occur directly adjacent to nucleosomes. The resulting hexasome-nucleosome complexes are then resolved by Chd1. We present two cryoelectron microscopy (cryo-EM) structures of Chd1 bound to a hexasome-nucleosome complex before and after restoration of the missing inner H2A/H2B dimer by FACT. Chd1 uniquely interacts with the complex, positioning its ATPase domain to shift the hexasome away from the nucleosome. In the absence of the inner H2A/H2B dimer, its DNA-binding domain (DBD) packs against the ATPase domain, suggesting an inhibited state. Restoration of the dimer by FACT triggers a rearrangement that displaces the DBD and stimulates Chd1 remodeling. Our results demonstrate how chromatin remodelers interact with a complex nucleosome assembly and suggest how Chd1 and FACT jointly support transcription by RNAPII.

PubMed: 39270644
DOI: 10.1016/j.molcel.2024.08.022

実験手法

ELECTRON MICROSCOPY (4.2 Å)