ArticleStructure (London, England : 1993)2011
NusA interaction with the α subunit of E. coli RNA polymerase is via the UP element site and releases autoinhibition.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 38 citations in OpenAlex.
- A complex between IF2 and NusA suggests early coupling of transcription-translation.Nature communications · 2025Article
- Inhibition of bacterial RNA polymerase function and protein-protein interactions: a promising approach for next-generation antibacterial therapeutics.RSC medicinal chemistry · 2024Review
- Transcription complexes as RNA chaperones.Transcription · 2021Article
- Macromolecular assemblies supporting transcription-translation coupling.Transcription · 2021Review
- Pre-termination Transcription Complex: Structure and Function.Molecular cell · 2021Article
- Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.Science (New York, N.Y.) · 2021Article
- Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- In-cell architecture of an actively transcribing-translating expressome.Science (New York, N.Y.) · 2020Article
- NusA directly interacts with antitermination factor Q from phage λ.Scientific reports · 2020Article
- Mechanisms of Transcriptional Pausing in Bacteria.Journal of molecular biology · 2019Review
- SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA.Nucleic acids research · 2019Article
- Structural basis for the function of SuhB as a transcription factor in ribosomal RNA synthesis.Nucleic acids research · 2019Article
- Structural Basis for NusA Stabilized Transcriptional Pausing.Molecular cell · 2018Article
- Architecture of a transcribing-translating expressome.Science (New York, N.Y.) · 2017Article
- Transcription is regulated by NusA:NusG interaction.Nucleic acids research · 2016Article
- Nascent RNA length dictates opposing effects of NusA on antitermination.Nucleic acids research · 2016Article
- Transcription Elongation Factor NusA Is a General Antagonist of Rho-dependent Termination in Escherichia coli.The Journal of biological chemistry · 2016Article
- Determination of RNA polymerase binding surfaces of transcription factors by NMR spectroscopy.Scientific reports · 2015Article
- Exploring RNA polymerase regulation by NMR spectroscopy.Scientific reports · 2015Article
- Regulation of transcription elongation and termination.Biomolecules · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Elongating Escherichia coli RNAP is modulated by NusA protein. The C-terminal domain (CTD) of the RNAP α subunit (αCTD) interacts with the acidic CTD 2 (AR2) of NusA, releasing the autoinhibitory blockade of the NusA S1-KH1-KH2 motif and allowing NusA to bind nascent nut spacer RNA. We determined the solution conformation of the AR2:αCTD complex. The αCTD residues that interface with AR2 are identical to those that recognize UP promoter elements A nusA-ΔAR2 mutation does not affect UP-dependent rrnH transcription initiation in vivo. Instead, the mutation inhibits Rho-dependent transcription termination at phage λtR1, which lies adjacent to the λnutR sequence. The Rho-dependent λtimm terminator, which is not preceded by a λnut sequence, is fully functional. We propose that constitutive binding of NusA-ΔAR2 to λnutR occludes Rho. In addition, the mutation confers a dominant defect in exiting stationary phase.
Indexed as
Identifiers
What OpenQuestion holds
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.