ArticleProceedings of the National Academy of Sciences of the United States of America2019
Structural basis of Q-dependent antitermination.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Design and discovery of 'tug-of-war' riboswitches.bioRxiv : the preprint server for biology · 2026Article
- A prophage intercepts pathogenic activity of infecting phage for defense.Cell host & microbe · 2025Article
- Article
- Rho-dependent transcription termination: mechanisms and roles in bacterial fitness and adaptation to environmental changes.RNA (New York, N.Y.) · 2025Review
- A phage transcription factor displaces the host σ factor and stabilizes its own σ factor.Nucleic acids research · 2025Article
- The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization.Nature communications · 2025Article
- Transcription termination and antitermination are critical for the fitness and function of the integrative and conjugative element Tn916.PLoS genetics · 2024Article
- An ensemble of interconverting conformations of the elemental paused transcription complex creates regulatory options.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Hybrid Vigor: Importance of Hybrid λ Phages in Early Insights in Molecular Biology.Microbiology and molecular biology reviews : MMBR · 2022Review
- Influence ofViruses · 2022Article
- In transcription antitermination by Qλ, NusA induces refolding of Qλ to form a nozzle that extends the RNA polymerase RNA-exit channel.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of transcriptional regulation by a nascent RNA element, HK022 putRNA.Nature communications · 2022Article
- Structural basis of AlpA-dependent transcription antitermination.Nucleic acids research · 2022Article
- Structural advances in transcription elongation.Current opinion in structural biology · 2022Review
- Structural and mechanistic basis of σ-dependent transcriptional pausing.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Transcription factors modulate RNA polymerase conformational equilibrium.Nature communications · 2022Article
- Structural and mechanistic basis of reiterative transcription initiation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular Modeling the Proteins from theAntibiotics (Basel, Switzerland) · 2021Review
- Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.Nucleic acids research · 2021Article
- Transcription complexes as RNA chaperones.Transcription · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
Lambdoid bacteriophage Q protein mediates the switch from middle to late bacteriophage gene expression by enabling RNA polymerase (RNAP) to read through transcription terminators preceding bacteriophage late genes. Q loads onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element (SDPE) to yield a Q-loading complex, and Q subsequently translocates with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. Here, we report high-resolution structures of 4 states on the pathway of antitermination by Q from bacteriophage 21 (Q21): Q21, the Q21-QBE complex, the Q21-loading complex, and the Q21-loaded complex. The results show that Q21 forms a torus, a "nozzle," that narrows and extends the RNAP RNA-exit channel, extruding topologically linked single-stranded RNA and preventing the formation of pause and terminator hairpins.
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