ArticleJournal of bacteriology2003
Leucines 193 and 194 at the N-terminal domain of the XylS protein, the positive transcriptional regulator of the TOL meta-cleavage pathway, are involved in dimerization.
Article in Journal of bacteriology, 2003. 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, 43 citations in OpenAlex.
- Elucidation of the DNA-Binding Activity of VirF from Shigella flexneri for theJournal of bacteriology · 2023Article
- HilD, HilC, and RtsA Form Homodimers and Heterodimers To Regulate Expression of theJournal of bacteriology · 2020Article
- Physical decoupling of XylS/Pm regulatory elements and conditional proteolysis enable precise control of gene expression in Pseudomonas putida.Microbial biotechnology · 2020Article
- 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
- A large family of anti-activators accompanying XylS/AraC family regulatory proteins.Molecular microbiology · 2016Article
- Article
- Benzoic Acid-Inducible Gene Expression in Mycobacteria.PloS one · 2015Article
- Self-association is required for occupation of adjacent binding sites in Pseudomonas aeruginosa type III secretion system promoters.Journal of bacteriology · 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
- Article
- Mutational analysis of the N-terminal domain of UreR, the positive transcriptional regulator of urease gene expression.Microbiological research · 2012Article
- 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
- Positively regulated bacterial expression systems.Microbial biotechnology · 2009Review
- Roles of effectors in XylS-dependent transcription activation: intramolecular domain derepression and DNA binding.Journal of bacteriology · 2008Article
- Residues near the amino terminus of Rns are essential for positive autoregulation and DNA binding.Journal of bacteriology · 2008Article
- The chaperone IpgC copurifies with the virulence regulator MxiE.Journal of bacteriology · 2008Article
- The TodS-TodT two-component regulatory system recognizes a wide range of effectors and works with DNA-bending proteins.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans.Journal of bacteriology · 2005Article
- Bacterial transcriptional regulators for degradation pathways of aromatic compounds.Microbiology and molecular biology reviews : MMBR · 2004Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the AraC/XylS family of transcriptional regulators are usually organized in two domains: a conserved domain made up of 100 amino acids and frequently located at the C-terminal end, involved in DNA binding; and an N-terminal nonconserved domain involved in signal recognition, as is the case for regulators involved in the control of carbon metabolism (R. Tobes and J. L. Ramos, Nucleic Acids Res. 30:318-321, 2002). The XylS protein, which is extremely insoluble, controls expression of the meta-cleavage pathway for alkylbenzoate metabolism. We fused the N-terminal end of XylS to the maltose-binding protein (MBP) in vitro and found in glutaraldehyde cross-linking assays that the protein dimerized. Experiments with a chimeric N-terminal XylS linked to a 'LexA protein showed that the dimer was stabilized in the presence of alkylbenzoates. Sequence alignments with AraC and UreR allowed us to identify three residues, Leu193, Leu194, and Ile205, as potentially being involved in dimerization. Site-directed mutagenesis of XylS in which each of the above residues was replaced with Ala revealed that Leu193 and Leu194 were critical for activity and that a chimera in which LexA was linked to the N terminus of XylSLeu193Ala or XylSLeu194Ala was not functional. Dimerization of the chimeras MBP-N-XylSLeu193Ala and MBP-N-XylSLeu194Ala was not observed in cross-linking assays with glutaraldehyde.
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