ArticleScientific reports2015
Determination of RNA polymerase binding surfaces of transcription factors by NMR spectroscopy.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Inhibition of bacterial RNA polymerase function and protein-protein interactions: a promising approach for next-generation antibacterial therapeutics.RSC medicinal chemistry · 2024Review
- Macromolecular assemblies supporting transcription-translation coupling.Transcription · 2021Review
- An in vitro reconstituted U1 snRNP allows the study of the disordered regions of the particle and the interactions with proteins and ligands.Nucleic acids research · 2021Article
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- Escherichia coli NusG Links the Lead Ribosome with the Transcription Elongation Complex.iScience · 2020Article
- NusA directly interacts with antitermination factor Q from phage λ.Scientific reports · 2020Article
- Spatial organization of RNA polymerase and its relationship with transcription inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA.Nucleic acids research · 2019Article
- Two Old Dogs, One New Trick: A Review of RNA Polymerase and Ribosome Interactions during Transcription-Translation Coupling.International journal of molecular sciences · 2019Review
- Reversible fold-switching controls the functional cycle of the antitermination factor RfaH.Nature communications · 2019Article
- Structural Basis for NusA Stabilized Transcriptional Pausing.Molecular cell · 2018Article
- Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.Nucleic acids research · 2017Article
- Mechanistic insights into transcription coupled DNA repair.DNA repair · 2017Review
- Structural basis for λN-dependent processive transcription antitermination.Nature microbiology · 2017Article
- Article
- Article
- Transcription Regulation in Archaea.Journal of bacteriology · 2016Review
- 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
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, RNA polymerase (RNAP), the central enzyme of transcription, is regulated by N-utilization substance (Nus) transcription factors. Several of these factors interact directly, and only transiently, with RNAP to modulate its function. As details of these interactions are largely unknown, we probed the RNAP binding surfaces of Escherichia coli (E. coli) Nus factors by nuclear magnetic resonance (NMR) spectroscopy. Perdeuterated factors with [(1)H,(13)C]-labeled methyl groups of Val, Leu, and Ile residues were titrated with protonated RNAP. After verification of this approach with the N-terminal domain (NTD) of NusG and RNAP we determined the RNAP binding site of NusE. It overlaps with the NusE interaction surface for the NusG C-terminal domain, indicating that RNAP and NusG compete for NusE and suggesting possible roles for the NusE:RNAP interaction, e.g. in antitermination and direct transcription:translation coupling. We solved the solution structure of NusA-NTD by NMR spectroscopy, identified its RNAP binding site with the same approach we used for NusG-NTD, and here present a detailed model of the NusA-NTD:RNAP:RNA complex.
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