EMD-22114
CryoEM Structure of E. coli Rho-dependent Transcription Pre-termination Complex
EMD-22114
Single-particle3.8 Å
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Map released: 16/12/2020
Last modified: 06/03/2024
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
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.
Hao Z
,
Epshtein V,
Kim KH,
Proshkin S
,
Svetlov V,
Kamarthapu V,
Bharati B,
Mironov A,
Walz T
,
Nudler E
(2021) Mol Cell , 81 , 281
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(2021) Mol Cell , 81 , 281
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.
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.