ArticleProceedings of the National Academy of Sciences of the United States of America2013
Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
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109 citing papers in PubMed, 168 citations in OpenAlex.
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- Phage portal proteins counteract stringent-response-mediated restriction.Nature communications · 2026Article
- Structural basis for multi-subunit DNA-dependent RNA polymerase catalytic activity.Molecular cell · 2026Article
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- Real-time capture of σNature communications · 2025Article
- Recent advances in mycobacterial transcription: insights beyond the general pathway.Journal of bacteriology · 2025Review
- A phage transcription factor displaces the host σ factor and stabilizes its own σ factor.Nucleic acids research · 2025Article
- RapA opens the RNA polymerase clamp to disrupt post-termination complexes and prevent cytotoxic R-loop formation.Nature structural & molecular biology · 2025Article
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.Nature structural & molecular biology · 2024Article
- Evidence for a compact σiScience · 2024Article
- Structural basis of promoter recognition by Staphylococcus aureus RNA polymerase.Nature communications · 2024Article
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.bioRxiv : the preprint server for biology · 2024Article
- Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.Biomolecules · 2023Article
- AInternational journal of molecular sciences · 2023Article
- Transcriptional pause extension benefits the stand-by rather than catch-up Rho-dependent termination.Nucleic acids research · 2023Article
- 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
- How to Shut Down Transcription in Archaea during Virus Infection.Microorganisms · 2022Review
- Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding.Nature communications · 2022Article
- Article
49 more citing papers are in PubMed but not listed here.
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6 authors at 3 institutions in 2 countries.
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Abstract
Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP σ(70) subunit domain 1.1(σ(1.1)(70)) inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with σ(1.1)(70), preventing the normal egress of σ(1.1)(70) from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, σ(1.1)(70), to inhibit the function of the enzyme.
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