ArticleNature communications2019
Structural basis of Q-dependent transcription antitermination.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
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- A prophage intercepts pathogenic activity of infecting phage for defense.Cell host & microbe · 2025Article
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- 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
- Structural insights into transcription regulation of the global OmpR/PhoB family regulator PhoP from Mycobacterium tuberculosis.Nature communications · 2025Article
- The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization.Nature communications · 2025Article
- Control of a gene transfer agent cluster in Caulobacter crescentus by transcriptional activation and anti-termination.Nature communications · 2024Article
- Structural and functional insights into transcription activation of the essential LysR-type transcriptional regulators.Protein science : a publication of the Protein Society · 2024Article
- DUF2285 is a novel helix-turn-helix domain variant that orchestrates both activation and antiactivation of conjugative element transfer in proteobacteria.Nucleic acids research · 2023Article
- Structural basis for control of bacterial RNA polymerase pausing by a riboswitch and its ligand.Nature structural & molecular biology · 2023Article
- Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of three different transcription activation strategies adopted by a single regulator SoxS.Nucleic acids research · 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 AlpA-dependent transcription antitermination.Nucleic acids research · 2022Article
- Structural basis of Streptomyces transcription activation by zinc uptake regulator.Nucleic acids research · 2022Article
- Structural basis of transcription activation by Rob, a pleiotropic AraC/XylS family regulator.Nucleic acids research · 2022Article
- Structural and mechanistic basis of σ-dependent transcriptional pausing.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of transcription activation by the global regulator Spx.Nucleic acids research · 2021Article
- Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q
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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.