ArticleJournal of bacteriology2007
Transcription activation by the DNA-binding domain of the AraC family protein RhaS in the absence of its effector-binding domain.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
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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.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
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- A genetically encoded L-rhamnose biosensor for monitoring marine polysaccharide depolymerization.Applied microbiology and biotechnology · 2026Article
- Establishing a Malonyl-CoA Biosensor for the Two Model CyanobacteriaACS synthetic biology · 2025Article
- Nucleotide-level characterization and improvement of l-arabinose- and l-rhamnose-inducible systems in E. coli using a high-throughput approach.Nucleic acids research · 2025Article
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- Improved Dynamic Range of a Rhamnose-Inducible Promoter for Gene Expression inApplied and environmental microbiology · 2021Article
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- Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli.Journal of bacteriology · 2013Article
- Identification of a small-molecule inhibitor of bacterial AraC family activators.Journal of biomolecular screening · 2013Article
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- Mutational analysis of the N-terminal domain of UreR, the positive transcriptional regulator of urease gene expression.Microbiological research · 2012Article
- In vitro transcription profiling of the σS subunit of bacterial RNA polymerase: re-definition of the σS regulon and identification of σS-specific promoter sequence elements.Nucleic acids research · 2011Article
- Article
- Sequential XylS-CTD binding to the Pm promoter induces DNA bending prior to activation.Journal of bacteriology · 2010Article
- Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium.Journal of bacteriology · 2010Article
- The AraC/XylS family activator RhaS negatively autoregulates rhaSR expression by preventing cyclic AMP receptor protein activation.Journal of bacteriology · 2010Article
- Mechanism of transcriptional activation by Pseudomonas aeruginosa ExsA.Journal of bacteriology · 2009Article
- Direct stimulus perception and transcription activation by a membrane-bound DNA binding protein.Molecular microbiology · 2009Article
- Functional domains of ExsA, the transcriptional activator of the Pseudomonas aeruginosa type III secretion system.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Escherichia coli L-rhamnose-responsive transcription activators RhaS and RhaR both consist of two domains, a C-terminal DNA-binding domain and an N-terminal dimerization domain. Both function as dimers and only activate transcription in the presence of L-rhamnose. Here, we examined the ability of the DNA-binding domains of RhaS (RhaS-CTD) and RhaR (RhaR-CTD) to bind to DNA and activate transcription. RhaS-CTD and RhaR-CTD were both shown by DNase I footprinting to be capable of binding specifically to the appropriate DNA sites. In vivo as well as in vitro transcription assays showed that RhaS-CTD could activate transcription to high levels, whereas RhaR-CTD was capable of only very low levels of transcription activation. As expected, RhaS-CTD did not require the presence of L-rhamnose to activate transcription. The upstream half-site at rhaBAD and the downstream half-site at rhaT were found to be the strongest of the known RhaS half-sites, and a new putative RhaS half-site with comparable strength to known sites was identified. Given that cyclic AMP receptor protein (CRP), the second activator required for full rhaBAD expression, cannot activate rhaBAD expression in a DeltarhaS strain, it was of interest to test whether CRP could activate transcription in combination with RhaS-CTD. We found that RhaS-CTD allowed significant activation by CRP, both in vivo and in vitro, although full-length RhaS allowed somewhat greater CRP activation. We conclude that RhaS-CTD contains all of the determinants necessary for transcription activation by RhaS.
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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.