登録情報 データベース : EMDB  /  ID : EMD-40683タイトル High resolution structure of ESRRB nucleosome bound OCT4 at site a and site b   複合体 : Complex of ESRRB nucleosome bound to OCT4DNA : DNA (168-MER)DNA : DNA (168-MER)タンパク質・ペプチド : Maltodextrin-binding protein,POU domain, class 5, transcription factor 1タンパク質・ペプチド : Histone H3.1タンパク質・ペプチド : Histone H4タンパク質・ペプチド : Histone H2A type 2-Cタンパク質・ペプチド : Histone H2B type 2-Eタンパク質・ペプチド : ScFv /   /   /   /   /  機能・相同性 分子機能 ドメイン・相同性 構成要素 
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 ジャーナル : Mol Cell  /  年 : 2023タイトル : Structural mechanism of LIN28B nucleosome targeting by OCT4.著者 : Ruifang Guan  /  Tengfei Lian  /  Bing-Rui Zhou  /  David Wheeler  /  Yawen Bai  /  要旨 : 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  ... 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. 履歴 登録 2023年5月3日 - ヘッダ(付随情報) 公開 2023年6月28日 - マップ公開 2023年6月28日 - 更新 2024年11月13日 - 現状 2024年11月13日 処理サイト : RCSB /  状態 : 公開
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