6JNX

Cryo-EM structure of a Q-engaged arrested complex

6JNX の概要

• エントリーDOI: 10.2210/pdb6jnx/pdb
• EMDBエントリー: 9852
• 分子名称: DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• 機能のキーワード: rna polymerase, antitermination, transcription, dna, rna
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 542222.24

構造登録者

Feng, Y.,Shi, J. (登録日: 2019-03-18, 公開日: 2019-06-12, 最終更新日: 2024-03-27)

主引用文献

Shi, J.,Gao, X.,Tian, T.,Yu, Z.,Gao, B.,Wen, A.,You, L.,Chang, S.,Zhang, X.,Zhang, Y.,Feng, Y.
Structural basis of Q-dependent transcription antitermination.
Nat Commun, 10:2925-2925, 2019

PubMed Abstract: Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q and Q) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, Q forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well.

PubMed: 31266960
DOI: 10.1038/s41467-019-10958-8

実験手法

ELECTRON MICROSCOPY (4.08 Å)