ArticleProceedings of the National Academy of Sciences of the United States of America2016
Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
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 32 papers.
What it found
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Who cites it
32 citing papers in PubMed, 57 citations in OpenAlex.
- Measuring the Affinity of the Bacterial Rho Helicase for RNA Using a Double-Membrane Slot-Blot Filtration Assay.Methods in molecular biology (Clifton, N.J.) · 2027Article
- 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
- Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ.Nature communications · 2025Article
- The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization.Nature communications · 2025Article
- Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation.Nature communications · 2024Article
- Phase Variation of Flagella and Toxins in Clostridioides difficile is Mediated by Selective Rho-dependent Termination.Journal of molecular biology · 2024Article
- Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase fromScience advances · 2023Article
- Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein.International journal of molecular sciences · 2023Article
- Article
- Determining translocation orientations of nucleic acid helicases.Methods (San Diego, Calif.) · 2022Review
- Rho-dependent transcription termination proceeds via three routes.Nature communications · 2022Article
- Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism.Communications biology · 2022Article
- Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021Review
- Rho-dependent transcription termination: a revisionist view.Transcription · 2021Review
- Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.Science (New York, N.Y.) · 2021Article
- Crystal structure of the Escherichia coli transcription termination factor Rho.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Cryo-EM Structure of the Fork Protection Complex Bound to CMG at a Replication Fork.Molecular cell · 2020Article
- Different mechanisms for translocation by monomeric and hexameric helicases.Current opinion in structural biology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ring-shaped hexameric helicases and translocases support essential DNA-, RNA-, and protein-dependent transactions in all cells and many viruses. How such systems coordinate ATPase activity between multiple subunits to power conformational changes that drive the engagement and movement of client substrates is a fundamental question. Using the Escherichia coli Rho transcription termination factor as a model system, we have used solution and crystallographic structural methods to delineate the range of conformational changes that accompany distinct substrate and nucleotide cofactor binding events. Small-angle X-ray scattering data show that Rho preferentially adopts an open-ring state in solution and that RNA and ATP are both required to cooperatively promote ring closure. Multiple closed-ring structures with different RNA substrates and nucleotide occupancies capture distinct catalytic intermediates accessed during translocation. Our data reveal how RNA-induced ring closure templates a sequential ATP-hydrolysis mechanism, provide a molecular rationale for how the Rho ATPase domains distinguishes between distinct RNA sequences, and establish structural snapshots of substepping events in a hexameric helicase/translocase.
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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.