8W8D

Structural mechanism of inhibition of the Rho transcription termination factor by Rof

Summary for 8W8D

• Entry DOI: 10.2210/pdb8w8d/pdb
• EMDB information: 37342
• Descriptor: Transcription termination factor Rho, Protein rof (3 entities in total)
• Functional Keywords: escherichia coli rho-rof complex, rho-dependent termination, antitermination, transcription
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 12
• Total formula weight: 339364.78

Authors

Zhang, J.,Wang, C. (deposition date: 2023-09-01, release date: 2024-05-01)

Primary citation

Zhang, J.,Zhang, S.,Zhou, W.,Zhang, X.,Li, G.,Li, R.,Lin, X.,Chen, Z.,Liu, F.,Shen, P.,Zhou, X.,Gao, Y.,Chen, Z.,Chao, Y.,Wang, C.
A widely conserved protein Rof inhibits transcription termination factor Rho and promotes Salmonella virulence program.
Nat Commun, 15:3187-3187, 2024

PubMed Abstract: Transcription is crucial for the expression of genetic information and its efficient and accurate termination is required for all living organisms. Rho-dependent termination could rapidly terminate unwanted premature RNAs and play important roles in bacterial adaptation to changing environments. Although Rho has been discovered for about five decades, the regulation mechanisms of Rho-dependent termination are still not fully elucidated. Here we report that Rof is a conserved antiterminator and determine the cryogenic electron microscopy structure of Rho-Rof antitermination complex. Rof binds to the open-ring Rho hexamer and inhibits the initiation of Rho-dependent termination. Rof's N-terminal α-helix undergoes conformational changes upon binding with Rho, and is key in facilitating Rof-Rho interactions. Rof binds to Rho's primary binding site (PBS) and excludes Rho from binding with PBS ligand RNA at the initiation step. Further in vivo analyses in Salmonella Typhimurium show that Rof is required for virulence gene expression and host cell invasion, unveiling a physiological function of Rof and transcription termination in bacterial pathogenesis.

PubMed: 38622116
DOI: 10.1038/s41467-024-47438-7

Experimental method

ELECTRON MICROSCOPY (2.8 Å)