ArticleProceedings of the National Academy of Sciences of the United States of America2016
Ligand-induced and small-molecule control of substrate loading in a hexameric helicase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Structure-to-function relationships of RNA polymerases: recent advances in bacterial transcription termination.Transcription · 2026Review
- Rho-dependent transcription termination: mechanisms and roles in bacterial fitness and adaptation to environmental changes.RNA (New York, N.Y.) · 2025Review
- NusG-Spt5 Transcription Factors: Universal, Dynamic Modulators of Gene Expression.Journal of molecular biology · 2025Review
- Crystal Structure and Mutagenesis of an XYP Subfamily Cyclodipeptide Synthase Reveal Key Determinants of Enzyme Activity and Substrate Specificity.Biochemistry · 2024Article
- Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation.Nature communications · 2024Article
- Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation.bioRxiv : the preprint server for biology · 2023Article
- Article
- RfaH May Oppose Silencing by H-NS and YmoA Proteins during Transcription Elongation.Journal of bacteriology · 2022Article
- Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism.Communications biology · 2022Article
- Rho-dependent transcription termination: a revisionist view.Transcription · 2021Review
- Modifications of diketopiperazines assembled by cyclodipeptide synthases with cytochrome PApplied microbiology and biotechnology · 2021Review
- Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.Science (New York, N.Y.) · 2021Article
- Tuning the sequence specificity of a transcription terminator.Current genetics · 2019Review
- Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.Molecular cell · 2018Article
- A multivariate prediction model for Rho-dependent termination of transcription.Nucleic acids research · 2018Article
- Recombinant yeast and human cells as screening tools to search for antibacterial agents targeting the transcription termination factor Rho.The Journal of antibiotics · 2018Article
- Identification of the Biosynthetic Pathway for the Antibiotic Bicyclomycin.Biochemistry · 2018Article
- A Bacteriophage Capsid Protein Is an Inhibitor of a Conserved Transcription Terminator of Various Bacterial Pathogens.Journal of bacteriology · 2018Article
- New Insights Into DNA Helicases as Druggable Targets for Cancer Therapy.Frontiers in molecular biosciences · 2018Review
- A Screen formBio · 2017Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Processive, ring-shaped protein and nucleic acid protein translocases control essential biochemical processes throughout biology and are considered high-prospect therapeutic targets. The Escherichia coli Rho factor is an exemplar hexameric RNA translocase that terminates transcription in bacteria. As with many ring-shaped motor proteins, Rho activity is modulated by a variety of poorly understood mechanisms, including small-molecule therapeutics, protein-protein interactions, and the sequence of its translocation substrate. Here, we establish the mechanism of action of two Rho effectors, the antibiotic bicyclomycin and nucleic acids that bind to Rho's primary RNA recruitment site. Using small-angle X-ray scattering and a fluorescence-based assay to monitor the ability of Rho to switch between open-ring (RNA-loading) and closed-ring (RNA-translocation) states, we found bicyclomycin to be a direct antagonist of ring closure. Reciprocally, the binding of nucleic acids to its N-terminal RNA recruitment domains is shown to promote the formation of a closed-ring Rho state, with increasing primary-site occupancy providing additive stimulatory effects. This study establishes bicyclomycin as a conformational inhibitor of Rho ring dynamics, highlighting the utility of developing assays that read out protein conformation as a prospective screening tool for ring-ATPase inhibitors. Our findings further show that the RNA sequence specificity used for guiding Rho-dependent termination derives in part from an intrinsic ability of the motor to couple the recognition of pyrimidine patterns in nascent transcripts to RNA loading and activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.