6A5L

RNA polymerase II elongation complex stalled at SHL(-1) of the nucleosome, with foreign DNA

6A5L の概要

• エントリーDOI: 10.2210/pdb6a5l/pdb
• EMDBエントリー: 6980
• 分子名称: DNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (23 entities in total)
• 機能のキーワード: nucleosome, chromatin, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 25
• 化学式量合計: 774560.04

構造登録者

Kujirai, T.,Ehara, H.,Fujino, Y.,Shirouzu, M.,Sekine, S.,Kurumizaka, H. (登録日: 2018-06-24, 公開日: 2018-10-03, 最終更新日: 2024-03-27)

主引用文献

Kujirai, T.,Ehara, H.,Fujino, Y.,Shirouzu, M.,Sekine, S.I.,Kurumizaka, H.
Structural basis of the nucleosome transition during RNA polymerase II passage.
Science, 362:595-598, 2018

PubMed Abstract: Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo-electron microscopy structures of RNAPII-nucleosome complexes in which RNAPII pauses at the superhelical locations SHL(-6), SHL(-5), SHL(-2), and SHL(-1) of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, in which RNAPII gradually tears DNA from the histone surface while preserving the histone octamer. The nucleosomes in the SHL(-1) complexes are bound to a "foreign" DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.

PubMed: 30287617
DOI: 10.1126/science.aau9904

実験手法

ELECTRON MICROSCOPY (5.6 Å)