ArticleProtein science : a publication of the Protein Society2005
The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Transcription complexes as RNA chaperones.Transcription · 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
- NusA directly interacts with antitermination factor Q from phage λ.Scientific reports · 2020Article
- 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
- 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
- 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
- An autoinhibited state in the structure of Thermotoga maritima NusG.Structure (London, England : 1993) · 2013Article
- Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity.Scientific reports · 2013Article
- NusA interaction with the α subunit of E. coli RNA polymerase is via the UP element site and releases autoinhibition.Structure (London, England : 1993) · 2011Article
- The role of E. coli Nus-factors in transcription regulation and transcription:translation coupling: From structure to mechanism.Transcription · 2011Article
- The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase.Journal of molecular biology · 2010Article
- RNA-binding specificity of E. coli NusA.Nucleic acids research · 2009Article
- Protein disorder is positively correlated with gene expression in Escherichia coli.Journal of proteome research · 2008Article
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5 authors.
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Abstract
The carboxy-terminal domain of the transcription factor Escherichia coli NusA, NusACTD, interacts with the protein N of bacteriophage lambda, lambdaN, and the carboxyl terminus of the E. coli RNA polymerase alpha subunit, alphaCTD. We solved the solution structure of the unbound NusACTD with high-resolution nuclear magnetic resonance (NMR). Additionally, we investigated the binding sites of lambdaN and alphaCTD on NusACTD using NMR titrations. The solution structure of NusACTD shows two structurally similar subdomains, NusA(353-416) and NusA(431-490), matching approximately two homologous acidic sequence repeats. Further characterization of NusACTD with 15N NMR relaxation data suggests that the interdomain region is only weakly structured and that the subdomains are not interacting. Both subdomains adopt an (HhH)2 fold. These folds are normally involved in DNA-protein and protein-protein interactions. NMR titration experiments show clear differences of the interactions of these two domains with alphaCTD and lambdaN, in spite of their structural similarity.
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