7OHC

Cryo-EM structure of nucleosome core particle composed of the Widom 601 DNA sequence

7OHC の概要

• エントリーDOI: 10.2210/pdb7ohc/pdb
• EMDBエントリー: 12900
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (6 entities in total)
• 機能のキーワード: nucleosome, nuclear 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: 10
• 化学式量合計: 197652.35

構造登録者

Wang, H.,Cramer, P. (登録日: 2021-05-10, 公開日: 2021-07-28, 最終更新日: 2024-07-10)

主引用文献

Wang, H.,Xiong, L.,Cramer, P.
Structures and implications of TBP-nucleosome complexes.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The TATA box-binding protein (TBP) is highly conserved throughout eukaryotes and plays a central role in the assembly of the transcription preinitiation complex (PIC) at gene promoters. TBP binds and bends DNA, and directs adjacent binding of the transcription factors TFIIA and TFIIB for PIC assembly. Here, we show that yeast TBP can bind to a nucleosome containing the Widom-601 sequence and that TBP-nucleosome binding is stabilized by TFIIA. We determine three cryo-electron microscopy (cryo-EM) structures of TBP-nucleosome complexes, two of them containing also TFIIA. TBP can bind to superhelical location (SHL) -6, which contains a TATA-like sequence, but also to SHL +2, which is GC-rich. Whereas binding to SHL -6 can occur in the absence of TFIIA, binding to SHL +2 is only observed in the presence of TFIIA and goes along with detachment of upstream terminal DNA from the histone octamer. TBP-nucleosome complexes are sterically incompatible with PIC assembly, explaining why a promoter nucleosome generally impairs transcription and must be moved before initiation can occur.

PubMed: 34301908
DOI: 10.1073/pnas.2108859118

実験手法

ELECTRON MICROSCOPY (2.5 Å)