8E70

Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, dC75 rut mimic RNA, Mg-ADP-BeF3, and NusG; Rho hexamer part

8E70 の概要

• エントリーDOI: 10.2210/pdb8e70/pdb
• EMDBエントリー: 27932
• 分子名称: dC75 RNA, Transcription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: factor-dependent termination, rho, transcription termination, transcription elongation complex, helicase, atpase, transcription-rna complex, transcription/rna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 308386.54

構造登録者

Molodtsov, V.,Wang, C.,Ebright, R.H. (登録日: 2022-08-23, 公開日: 2022-09-07, 最終更新日: 2024-06-19)

主引用文献

Molodtsov, V.,Wang, C.,Firlar, E.,Kaelber, J.T.,Ebright, R.H.
Structural basis of Rho-dependent transcription termination.
Nature, 614:367-374, 2023

PubMed Abstract: Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription-translation-coupling quality control in Escherichia coli. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho's function.

PubMed: 36697824
DOI: 10.1038/s41586-022-05658-1

実験手法

ELECTRON MICROSCOPY (4.1 Å)