EMD-22114

Single-particle
3.8 Å
EMD-22114 Deposition: 04/06/2020
Map released: 16/12/2020
Last modified: 06/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-22114

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

EMD-22114

Single-particle
3.8 Å
EMD-22114 Deposition: 04/06/2020
Map released: 16/12/2020
Last modified: 06/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Escherichia coli (strain K12)
Sample: E. coli Rho-dependent Transcription Pre-termination Complex
Fitted models: 6xas (Avg. Q-score: 0.334)

Deposition Authors: Hao ZT, Kim HK
Pre-termination Transcription Complex: Structure and Function.
PUBMED: 33296676
DOI: doi:10.1016/j.molcel.2020.11.013
ISSN: 1097-2765
ASTM: MOCEFL
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.