8DK5

Structure of 187bp LIN28b nucleosome with site 0 mutation

8DK5 の概要

• エントリーDOI: 10.2210/pdb8dk5/pdb
• 関連するPDBエントリー: 7U0G 7U0I 7U0J
• EMDBエントリー: 27483
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 2-C, ... (7 entities in total)
• 機能のキーワード: nucleosome, transcription, chromatin binding protein-dna complex, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 283099.68

構造登録者

Lian, T.,Guan, R.,Bai, Y. (登録日: 2022-07-02, 公開日: 2023-06-28, 最終更新日: 2024-11-13)

主引用文献

Guan, R.,Lian, T.,Zhou, B.R.,Wheeler, D.,Bai, Y.
Structural mechanism of LIN28B nucleosome targeting by OCT4.
Mol.Cell, 83:1970-1982.e6, 2023

PubMed Abstract: Pioneer transcription factors are essential for cell fate changes by targeting closed chromatin. OCT4 is a crucial pioneer factor that can induce cell reprogramming. However, the structural basis of how pioneer factors recognize the in vivo nucleosomal DNA targets is unknown. Here, we determine the high-resolution structures of the nucleosome containing human LIN28B DNA and its complexes with the OCT4 DNA binding region. Three OCT4s bind the pre-positioned nucleosome by recognizing non-canonical DNA sequences. Two use their POUS domains while the other uses the POUS-loop-POUHD region; POUHD serves as a wedge to unwrap ∼25 base pair DNA. Our analysis of previous genomic data and determination of the ESRRB-nucleosome-OCT4 structure confirmed the generality of these structural features. Moreover, biochemical studies suggest that multiple OCT4s cooperatively open the H1-condensed nucleosome array containing the LIN28B nucleosome. Thus, our study suggests a mechanism of how OCT4 can target the nucleosome and open closed chromatin.

PubMed: 37327775
DOI: 10.1016/j.molcel.2023.05.030

実験手法

ELECTRON MICROSCOPY (2.71 Å)