Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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.

Journal of bacteriology - 1 Jul 1990

Zhou L M, Timmis K N, Ramos J L

Abstract excerpt

The XylS protein is the positive activator of the TOL plasmid meta-cleavage pathway operon for the metabolism of alkylbenzoates in Pseudomonas putida. The regulator stimulates transcription from the TOL meta pathway operon promoter (Pm) when activated by benzoate effectors or in the absence of effectors when overproduced. xylS mutant alleles that encode regulators which constitutively mediate expression from Pm...

Topics

Alleles
Bacterial Proteins
Benzoates
Chromosome Mapping
Escherichia coli
Mutation
Operon
Plasmids
Pseudomonas
Transcription, Genetic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 2193914
DOI: 10.1128/jb.172.7.3707-3710.1990
PMCID: PMC213347

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2193914-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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.PMID 2193914Read ↗

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 ↗

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

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

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

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 ↗

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

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 ↗

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

⌁Select a neighboring publication to make it the new centre.