8HSH

Thermus thermophilus RNA polymerase coreenzyme

Summary for 8HSH

• Entry DOI: 10.2210/pdb8hsh/pdb
• Related: 8HSG 8HSJ 8HSL 8HSR
• EMDB information: 34996 34997 34999 35000 35004
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (6 entities in total)
• Functional Keywords: rna polymerase coreenzyme, transcription
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 5
• Total formula weight: 379189.62

Authors

Murayama, Y.,Ehara, H.,Sekine, S. (deposition date: 2022-12-19, release date: 2023-05-03, Last modification date: 2024-07-03)

Primary citation

Murayama, Y.,Ehara, H.,Aoki, M.,Goto, M.,Yokoyama, T.,Sekine, S.I.
Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from Thermus thermophilus.
Sci Adv, 9:eade7093-eade7093, 2023

PubMed 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 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.

PubMed: 36753546
DOI: 10.1126/sciadv.ade7093

Experimental method

ELECTRON MICROSCOPY (3.4 Å)