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Article

XylS domain interactions can be deduced from intraallelic dominance in double mutants of Pseudomonas putida.

Molecular & general genetics : MGG - 1 Nov 1992

Michán C, Kessler B, de Lorenzo V, Timmis K N, Ramos J L

Abstract excerpt

The XylS protein is the positive regulator of the TOL plasmid-encoded meta-cleavage pathway for the metabolism of alkylbenzoates in Pseudomonas putida. This protein is activated by a variety of benzoate analogues. To elucidate the functional domains of the regulator and their interactions, several fusions of the XylS C-terminus to MS2 polymerase and of the N-terminus to beta-galactosidase were constructed but all...

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Identifiers

PMID: 1465113
DOI: 10.1007/BF00279387

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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XylS domain interactions can be deduced from intraallelic dominance in double mutants of Pseudomonas putida.PMID 1465113Read ↗

Mutations leading to constitutive expression from the TOL plasmid meta-cleavage pathway operon are located at the C-terminal end of the positive regulator protein XylS.Semantic proximity Read ↗

Identification of critical amino-terminal regions of XylS. The positive regulator encoded by the TOL plasmid.Semantic proximity Read ↗

Signal-regulator interactions. Genetic analysis of the effector binding site of xylS, the benzoate-activated positive regulator of Pseudomonas TOL plasmid meta-cleavage pathway operon.Semantic proximity Read ↗

The organization of the Pm promoter of the TOL plasmid reflects the structure of its cognate activator protein XylS.Semantic proximity Read ↗

Cross talk between catabolic pathways in Pseudomonas putida: XylS-dependent and -independent activation of the TOL meta operon requires the same cis-acting sequences within the Pm promoter.Semantic proximity Read ↗

XylS-Pm promoter interactions through two helix-turn-helix motifs: identifying XylS residues important for DNA binding and activation.Semantic proximity Read ↗

Residues 137 and 153 of XylS influence contacts with the C-terminal domain of the RNA polymerase alpha subunit.Semantic proximity Read ↗

Switching the Ligand Specificity of the Biosensor XylS from meta to para-Toluic Acid through Directed Evolution Exploiting a Dual Selection System.Semantic proximity Read ↗

Residues 137 and 153 at the N terminus of the XylS protein influence the effector profile of this transcriptional regulator and the sigma factor used by RNA polymerase to stimulate transcription from its cognate promoter.Semantic proximity Read ↗

Mutational analysis of the highly conserved C-terminal residues of the XylS protein, a member of the AraC family of transcriptional regulators.Semantic proximity Read ↗

Engineering of the Ligand Specificity of Transcriptional Regulator XylS by Deep Mutational Scanning.Semantic proximity Read ↗

Allosteric regulation within the highly interconnected structural scaffold of AraC/XylS homologs tolerates a wide range of amino acid changes.Semantic proximity Read ↗

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