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Article

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

The Journal of biological chemistry - 15 Nov 1992

Michan C, Zhou L, Gallegos M T, Timmis K N, Ramos J L

Abstract excerpt

The XylS protein is the positive regulator of the promoter controlling the meta-cleavage pathway (Pm) for catabolism of certain alkylbenzoates on the TOL plasmid of Pseudomonas. Transcription from Pm is mediated by XylS either in the presence of benzoate effectors or through XylS hyperproduction. Two regions of the NH2 terminus of XylS (residues 37-45) had been predicted to be involved in effector control of XylS...

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Source

Identifiers

PMID: 1429638

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Click a neighbor to travelStep 1 · 12 closest

Identification of critical amino-terminal regions of XylS. The positive regulator encoded by the TOL plasmid.PMID 1429638Read ↗

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 ↗

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

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 ↗

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

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

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 ↗

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 ↗

A T7 RNA polymerase-based system for the construction of Pseudomonas strains with phenotypes dependent on TOL-meta pathway effectors.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 ↗

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