6XAS

CryoEM Structure of E. coli Rho-dependent Transcription Pre-termination Complex

6XAS の概要

• エントリーDOI: 10.2210/pdb6xas/pdb
• EMDBエントリー: 22114 22115
• 分子名称: Transcription termination/antitermination protein NusA, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• 機能のキーワード: rho-dependent transcription termination, transcription
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 764907.30

構造登録者

Hao, Z.T.,Kim, H.K.,Walz, T.,Nudler, E. (登録日: 2020-06-04, 公開日: 2020-12-16, 最終更新日: 2024-03-06)

主引用文献

Hao, Z.,Epshtein, V.,Kim, K.H.,Proshkin, S.,Svetlov, V.,Kamarthapu, V.,Bharati, B.,Mironov, A.,Walz, T.,Nudler, E.
Pre-termination Transcription Complex: Structure and Function.
Mol.Cell, 81:281-, 2021

PubMed Abstract: Rho is a general transcription termination factor playing essential roles in RNA polymerase (RNAP) recycling, gene regulation, and genomic stability in most bacteria. Traditional models of transcription termination postulate that hexameric Rho loads onto RNA prior to contacting RNAP and then translocates along the transcript in pursuit of the moving RNAP to pull RNA from it. Here, we report the cryoelectron microscopy (cryo-EM) structures of two termination process intermediates. Prior to interacting with RNA, Rho forms a specific "pre-termination complex" (PTC) with RNAP and elongation factors NusA and NusG, which stabilize the PTC. RNA exiting RNAP interacts with NusA before entering the central channel of Rho from the distal C-terminal side of the ring. We map the principal interactions in the PTC and demonstrate their critical role in termination. Our results support a mechanism in which the formation of a persistent PTC is a prerequisite for termination.

PubMed: 33296676
DOI: 10.1016/j.molcel.2020.11.013

実験手法

ELECTRON MICROSCOPY (3.8 Å)