ArticleNucleic acids research2009
RNA-binding specificity of E. coli NusA.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- A nascent riboswitch helix orchestrates robust transcriptional regulation through signal integration.Nature communications · 2024Article
- Dynamic competition between a ligand and transcription factor NusA governs riboswitch-mediated transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 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
- Identification of Rumen Microbial Genes Involved in Pathways Linked to Appetite, Growth, and Feed Conversion Efficiency in Cattle.Frontiers in genetics · 2019Article
- Identification of regulatory targets for the bacterial Nus factor complex.Nature communications · 2017Article
- Transcription is regulated by NusA:NusG interaction.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
- Bacteriophage lambda: Early pioneer and still relevant.Virology · 2015Review
- Regulation of Transcript Elongation.Annual review of microbiology · 2015Review
- Bacteriophage HK022 Nun protein arrests transcription by blocking lateral mobility of RNA polymerase during transcription elongation.Bacteriophage · 2014Article
- Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity.Scientific reports · 2013Article
- Nus transcription elongation factors and RNase III modulate small ribosome subunit biogenesis in Escherichia coli.Molecular microbiology · 2013Article
- A multipronged strategy of an anti-terminator protein to overcome Rho-dependent transcription termination.Nucleic acids research · 2012Article
- Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis.Journal of Zhejiang University. Science. B · 2011Article
- Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination.Nucleic acids research · 2011Article
- 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
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Authors and funding
6 authors.
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Abstract
The RNA sequences boxA, boxB and boxC constitute the nut regions of phage lambda. They nucleate the formation of a termination-resistant RNA polymerase complex on the lambda chromosome. The complex includes E. coli proteins NusA, NusB, NusG and NusE, and the lambda N protein. A complex that includes the Nus proteins and other factors forms at the rrn leader. Whereas RNA-binding by NusB and NusE has been described in quantitative terms, the interaction of NusA with these RNA sequences is less defined. Isotropic as well as anisotropic fluorescence equilibrium titrations show that NusA binds only the nut spacer sequence between boxA and boxB. Thus, nutR boxA5-spacer, nutR boxA16-spacer and nutR boxA69-spacer retain NusA binding, whereas a spacer mutation eliminates complex formation. The affinity of NusA for nutL is 50% higher than for nutR. In contrast, rrn boxA, which includes an additional U residue, binds NusA in the absence of spacer. The K(d) values obtained for rrn boxA and rrn boxA-spacer are 19-fold and 8-fold lower, respectively, than those for nutR boxA-spacer. These differences may explain why lambda requires an additional protein, lambda N, to suppress termination. Knowledge of the different affinities now describes the assembly of the anti-termination complex in quantitative terms.
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