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

A Free, R M Williams, C J Dorman

Research output: Contribution to journalArticlepeer-review

Abstract

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 to be necessary for repression, which is consistent with a role for StpA as a DNA-binding adapter for mutant derivatives of H-NS.

Original languageEnglish
Pages (from-to)994-7
Number of pages4
JournalJournal of Bacteriology
Volume180
Issue number4
Publication statusPublished - Feb 1998

Keywords

  • 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
  • Mutation
  • Operon
  • Peptide Fragments
  • Sequence Deletion

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