ArticleJournal of bacteriology2008
Residues near the amino terminus of Rns are essential for positive autoregulation and DNA binding.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Diversity in Genetic Regulation of Bacterial Fimbriae Assembled by the Chaperone Usher Pathway.International journal of molecular sciences · 2022Review
- Structure of the master regulator Rns reveals an inhibitor of enterotoxigenic Escherichia coli virulence regulons.Scientific reports · 2021Article
- The AraC-Type Transcriptional Regulator GliR (PA3027) Activates Genes of Glycerolipid Metabolism inInternational journal of molecular sciences · 2021Article
- The Salmonella Typhimurium InvF-SicA complex is necessary for the transcription of sopB in the absence of the repressor H-NS.PloS one · 2020Article
- Article
- Virulence regulons of enterotoxigenic Escherichia coli.Immunologic research · 2013Review
- Further characterization of functional domains of PerA, role of amino and carboxy terminal domains in DNA binding.PloS one · 2013Article
- Virulence regulation in Citrobacter rodentium: the art of timing.Microbial biotechnology · 2010Review
- Functional domains of ExsA, the transcriptional activator of the Pseudomonas aeruginosa type III secretion system.Journal of bacteriology · 2009Article
- Positively regulated bacterial expression systems.Microbial biotechnology · 2009Review
- Transcriptional regulation of subclass 5b fimbriae.BMC microbiology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Most members of the AraC/XylS family contain a conserved carboxy-terminal DNA binding domain and a less conserved amino-terminal domain involved in binding small-molecule effectors and dimerization. However, there is no evidence that Rns, a regulator of enterotoxigenic Escherichia coli virulence genes, responds to an effector ligand, and in this study we found that the amino-terminal domain of Rns does not form homodimers in vivo. Exposure of Rns to the chemical cross-linker glutaraldehyde revealed that the full-length protein is also a monomer in vitro. Nevertheless, deletion analysis of Rns demonstrated that the first 60 amino acids of the protein are essential for the activation and repression of Rns-regulated promoters in vivo. Amino-terminal truncation of Rns abolished DNA binding in vitro, and two randomly generated mutations, I14T and N16D, that independently abolished Rns autoregulation were isolated. Further analysis of these mutations revealed that they have disparate effects at other Rns-regulated promoters and suggest that they may be involved in an interaction with the carboxy-terminal domain of Rns. Thus, evolution may have preserved the amino terminus of Rns because it is essential for the regulator's activity even though it apparently lacks the two functions, dimerization and ligand binding, usually associated with the amino-terminal domains of AraC/XylS family members.
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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.