ArticleProceedings of the National Academy of Sciences of the United States of America2008
The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Single-molecule experiments reveal NusG displaces transcription initiation factor σ70 from mature elongation complexes.Nucleic acids research · 2026Article
- Sticking around: σ factor dynamics and implications for transcription elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- How do bacteria tune transcription termination efficiency?Current opinion in microbiology · 2024Review
- Metamorphic proteins under a computational microscope: Lessons from a fold-switching RfaH protein.Computational and structural biotechnology journal · 2022Review
- Article
- NusG, an Ancient Yet Rapidly Evolving Transcription Factor.Frontiers in microbiology · 2020Review
- Article
- Ancient Transcription Factors in the News.mBio · 2019Review
- Reading of the non-template DNA by transcription elongation factors.Molecular microbiology · 2018Article
- Locking the nontemplate DNA to control transcription.Molecular microbiology · 2018Article
- Article
- Article
- Review
- σ38-dependent promoter-proximal pausing by bacterial RNA polymerase.Nucleic acids research · 2017Article
- A global analysis of transcription reveals two modes of Spt4/5 recruitment to archaeal RNA polymerase.Nature microbiology · 2017Article
- Nascent RNA length dictates opposing effects of NusA on antitermination.Nucleic acids research · 2016Article
- Bacterial RNA polymerase can retain σ70 throughout transcription.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Ubiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigms.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
RNA polymerase is a target for numerous regulatory events in all living cells. Recent studies identified a few "hot spots" on the surface of bacterial RNA polymerase that mediate its interactions with diverse accessory proteins. Prominent among these hot spots, the beta' subunit clamp helices serve as a major binding site for the initiation factor sigma and for the elongation factor RfaH. Furthermore, the two proteins interact with the nontemplate DNA strand in transcription complexes and thus may interfere with each other's activity. We show that RfaH does not inhibit transcription initiation but, once recruited to RNA polymerase, abolishes sigma-dependent pausing. We argue that this apparent competition is due to a steric exclusion of sigma by RfaH that is stably bound to the nontemplate DNA and clamp helices, both of which are necessary for the sigma recruitment to the transcription complex. Our findings highlight the key regulatory role played by the clamp helices during both initiation and elongation stages of transcription.
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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.