Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2024 Apr 15;15:3187. doi: 10.1038/s41467-024-47438-7

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 2 — a Superposition of Rho-Rof antitermination complex with Rho-dependent pre-termination complex. Left panel, overall structures of Rho-dependent pre-termination complex with λtR1 rut RNA (λtR1-Rho-NusG-TEC). Rho, cyan; RNAP in TEC, grey; non-template strand DNA, template strand DNA, and RNA, black, blue, and brick-red, respectively; NusG, magenta. Right panel, exactly same view with left panel, each Rof-Rho protomer are superposed with structure of λtR1-Rho-NusG-TEC, and replaced λtR1 rut RNA with Rof. Rof, orange; other colors and labels are as left panel. b Details of interactions for Rof/λtR1 rut RNA with Rho protomers A-F. Rho residues that interact with PBS-ligand RNA are shown as cyan spheres. λtR1 rut RNA is shown as brick-red; Rof N-terminal α helix is shown as orange; the competing binding site of Rof and PBS-ligand RNA is marked by red asterisk. c Relative inhibition efficiency of Rof on Rho-dC34 complex identified by electrophoretic mobility shift assay. Substitutions of residues involved in Rof-Rho interactions suppressed Rof’s binding affinity with Rho thus decreased Rof’s inhibition efficiency on Rho-PBS ligand RNA (dC34) formation. Data for in vitro transcription assays are means of three technical replicates. Error bars represent ± SEM of n = 3 experiments. M3-1 represents N9A/D11A/D12A triple mutations, M3-2 represents R46A/K47A/N48A triple mutations. d Relative in vitro transcription activity with Rho and Rof. Substitutions of residues involved in Rof-Rho interactions suppressed Rof’s antitermination efficiency on Rho-dependent termination thus suppressed in vitro transcription activity. Data for in vitro transcription assays are means of three technical replicates. Error bars represent ± SEM of n = 3 experiments. M3-1 represents N9A/D11A/D12A triple mutations, M3-2 represents R46A/K47A/N48A triple mutations.