8E3H

Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG; Rho hexamer part

Summary for 8E3H

• Entry DOI: 10.2210/pdb8e3h/pdb
• EMDB information: 27864 27865 27913 27914 27915 27916 27917 27918
• Descriptor: RNA with 18 nt long spacer, Transcription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: factor-dependent termination, rho, transcription termination, transcription elongation complex, helicase, atpase, transcription-rna complex, transcription/rna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 7
• Total formula weight: 296601.41

Authors

Molodtsov, V.,Wang, C. (deposition date: 2022-08-17, release date: 2022-09-07, Last modification date: 2024-06-12)

Primary citation

Molodtsov, V.,Wang, C.,Firlar, E.,Kaelber, J.T.,Ebright, R.H.
Structural basis of Rho-dependent transcription termination.
Nature, 614:367-374, 2023

PubMed Abstract: Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription-translation-coupling quality control in Escherichia coli. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho's function.

PubMed: 36697824
DOI: 10.1038/s41586-022-05658-1

Experimental method

ELECTRON MICROSCOPY (6.5 Å)