7PY0

CryoEM structure of E.coli RNA polymerase elongation complex bound to NusG (NusG-EC in more-swiveled conformation)

7PY0 の概要

• エントリーDOI: 10.2210/pdb7py0/pdb
• EMDBエントリー: 13706
• 分子名称: ntDNA, ZINC ION, tDNA, ... (10 entities in total)
• 機能のキーワード: nusg, transcription elongation, cryo-em, transcription
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 438764.34

構造登録者

Zhu, C.,Guo, X.,Weixlbaumer, A. (登録日: 2021-10-08, 公開日: 2022-03-23, 最終更新日: 2024-07-17)

主引用文献

Zhu, C.,Guo, X.,Dumas, P.,Takacs, M.,Abdelkareem, M.,Vanden Broeck, A.,Saint-Andre, C.,Papai, G.,Crucifix, C.,Ortiz, J.,Weixlbaumer, A.
Transcription factors modulate RNA polymerase conformational equilibrium.
Nat Commun, 13:1546-1546, 2022

PubMed Abstract: RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind RNAP simultaneously. Here we report cryo-EM reconstructions of Escherichia coli RNAP bound to NusG, or NusA, or both. RNAP conformational changes, referred to as swivelling, correlate with transcriptional pausing. NusA facilitates RNAP swivelling to further increase pausing, while NusG counteracts this role. Their structural effects are consistent with biochemical results on two categories of transcriptional pauses. In addition, the structures suggest a cooperative mechanism of NusA and NusG during Rho-mediated transcription termination. Our results provide a structural rationale for the stochastic nature of pausing and termination and how NusA and NusG can modulate it.

PubMed: 35318334
DOI: 10.1038/s41467-022-29148-0

実験手法

ELECTRON MICROSCOPY (4.5 Å)