6XAS

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

Summary for 6XAS

• Entry DOI: 10.2210/pdb6xas/pdb
• EMDB information: 22114 22115
• Descriptor: Transcription termination/antitermination protein NusA, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• Functional Keywords: rho-dependent transcription termination, transcription
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 15
• Total formula weight: 764907.30

Authors

Hao, Z.T.,Kim, H.K.,Walz, T.,Nudler, E. (deposition date: 2020-06-04, release date: 2020-12-16, Last modification date: 2024-03-06)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.8 Å)