ArticleJournal of bacteriology2000
Functional domains of the TOL plasmid transcription factor XylS.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Improved Dynamic Range of a Rhamnose-Inducible Promoter for Gene Expression inApplied and environmental microbiology · 2021Article
- The XylS/Pm regulator/promoter system and its use in fundamental studies of bacterial gene expression, recombinant protein production and metabolic engineering.Microbial biotechnology · 2017Review
- Genetically modified microorganism Spingomonas paucimobilis UT26 for simultaneously degradation of methyl-parathion and γ-hexachlorocyclohexane.Ecotoxicology (London, England) · 2014Article
- Regulation of the expression level of transcription factor XylS reveals new functional insight into its induction mechanism at the Pm promoter.BMC microbiology · 2013Article
- Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli.Journal of bacteriology · 2013Article
- Sequential XylS-CTD binding to the Pm promoter induces DNA bending prior to activation.Journal of bacteriology · 2010Article
- Directed evolution of the transcription factor XylS for development of improved expression systems.Microbial biotechnology · 2010Article
- 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
- The beta-catenin/TCF4 pathway modifies alternative splicing through modulation of SRp20 expression.RNA (New York, N.Y.) · 2008Article
- Roles of effectors in XylS-dependent transcription activation: intramolecular domain derepression and DNA binding.Journal of bacteriology · 2008Article
- Differences in the mechanism of the allosteric l-rhamnose responses of the AraC/XylS family transcription activators RhaS and RhaR.Molecular microbiology · 2008Article
- Residues near the amino terminus of Rns are essential for positive autoregulation and DNA binding.Journal of bacteriology · 2008Article
- Transcription activation by the DNA-binding domain of the AraC family protein RhaS in the absence of its effector-binding domain.Journal of bacteriology · 2007Article
- Transcriptional activation of quinoline degradation operons of Pseudomonas putida 86 by the AraC/XylS-type regulator OxoS and cross-regulation of the PqorM promoter by XylS.Applied and environmental microbiology · 2005Article
- Bacterial transcriptional regulators for degradation pathways of aromatic compounds.Microbiology and molecular biology reviews : MMBR · 2004Review
- Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR.Journal of bacteriology · 2004Article
- Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1.Journal of bacteriology · 2003Article
- DNA binding of the transcription activator protein MelR from Escherichia coli and its C-terminal domain.Nucleic acids research · 2002Article
- Biodegradation of aromatic compounds by Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2001Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The alkylbenzoate degradation genes of Pseudomonas putida TOL plasmid are positively regulated by XylS, an AraC family protein, in a benzoate-dependent manner. In this study, we used deletion mutants and hybrid proteins to identify which parts of XylS are responsible for the DNA binding, transcriptional activation, and benzoate inducibility. We found that a 112-residue C-terminal fragment of XylS binds specifically to the Pm operator in vitro, protects this sequence from DNase I digestion identically to the wild-type (wt) protein, and activates the Pm promoter in vivo. When overexpressed, that C-terminal fragment could activate transcription as efficiently as wt XylS. All the truncations, which incorporated these 112 C-terminal residues, were able to activate transcription at least to some extent when overproduced. Intactness of the 210-residue N-terminal portion was found to be necessary for benzoate responsiveness of XylS. Deletions in the N-terminal and central regions seriously reduced the activity of XylS and caused the loss of effector control, whereas insertions into the putative interdomain region did not change the basic features of the XylS protein. Our results confirm that XylS consists of two parts which probably interact with each other. The C-terminal domain carries DNA-binding and transcriptional activation abilities, while the N-terminal region carries effector-binding and regulatory functions.
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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.