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Article

The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli.

Journal of bacteriology - 1 Feb 1998

Free A, Williams R M, Dorman C J

Abstract excerpt

The mechanism of repression of the beta-glucoside utilization (bgl) operon of Escherichia coli by a carboxy-terminally truncated derivative of the nucleoid-associated protein H-NS which is defective in DNA binding was investigated. The DNA-binding function of the H-NS-like protein StpA was found...

Topics

Amino Acid Transport Systems
Bacterial Proteins
Carrier Proteins
DNA-Binding Proteins
Enzyme Repression
Escherichia coli
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Genes, Reporter
Glucosides
Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Operon

Peptide Fragments

Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 9473058
DOI: 10.1128/JB.180.4.994-997.1998
PMCID: PMC106983

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9473058-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli.PMID 9473058Read ↗

Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein.Semantic proximity Read ↗

rpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli.Semantic proximity Read ↗

Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS.Semantic proximity Read ↗

A truncated H-NS-like protein from enteropathogenic Escherichia coli acts as an H-NS antagonist.Semantic proximity Read ↗

YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes with H-NS and StpA.Semantic proximity Read ↗

H-NS and H-NS-like proteins in Gram-negative bacteria and their multiple role in the regulation of bacterial metabolism.Semantic proximity Read ↗

The structural and functional organization of H-NS-like proteins is evolutionarily conserved in gram-negative bacteria.Semantic proximity Read ↗

Differential binding profiles of StpA in wild-type and h-ns mutant cells: a comparative analysis of cooperative partners by chromatin immunoprecipitation-microarray analysis.Semantic proximity Read ↗

The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions.Semantic proximity Read ↗

Promoter-specific repression of fimB expression by the Escherichia coli nucleoid-associated protein H-NS.Semantic proximity Read ↗

H-NS over-expression induces an artificial stationary phase by silencing global transcription.Semantic proximity Read ↗

The H-NS dimerization domain defines a new fold contributing to DNA recognition.Semantic proximity Read ↗

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