EMD-36745

Single-particle
4.6 Å
EMD-36745 Deposition: 05/07/2023
Map released: 16/08/2023
Last modified: 16/08/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-36745

Thermus thermophilus Rho-engaged RNAP elongation complex; Rho part

EMD-36745

Single-particle
4.6 Å
EMD-36745 Deposition: 05/07/2023
Map released: 16/08/2023
Last modified: 16/08/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Thermus thermophilus HB8
Sample: Rho-engaged RNA polymerase elongation complex; Rho part

Deposition Authors: Murayama Y , Ehara H , Sekine S
Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from
Murayama Y , Ehara H , Aoki M, Goto M , Yokoyama T , Sekine SI
(2023) Sci Adv , 9 , eade7093
PUBMED: 36753546
DOI: doi:10.1101/2022.08.29.505764
ISSN: 2375-2548
Abstract:
Transcription termination is an essential step in transcription by RNA polymerase (RNAP) and crucial for gene regulation. For many bacterial genes, transcription termination is mediated by the adenosine triphosphate-dependent RNA translocase/helicase Rho, which causes RNA/DNA dissociation from the RNAP elongation complex (EC). However, the structural basis of the interplay between Rho and RNAP remains obscure. Here, we report the cryo-electron microscopy structure of the Thermus thermophilus RNAP EC engaged with Rho. The Rho hexamer binds RNAP through the carboxyl-terminal domains, which surround the RNA exit site of RNAP, directing the nascent RNA seamlessly from the RNA exit to its central channel. The β-flap tip at the RNA exit is critical for the Rho-dependent RNA release, and its deletion causes an alternative Rho-RNAP binding mode, which is irrelevant to termination. The Rho binding site overlaps with the binding sites of other macromolecules, such as ribosomes, providing a general basis of gene regulation.