Article
rpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli.
Journal of bacteriology - 1 Oct 1999
Ohta T, Ueguchi C, Mizuno T
Abstract excerpt
From evolutionary and physiological viewpoints, the Escherichia coli bgl operon is intriguing because its expression is silent (Bgl(-) phenotype), at least under several laboratory conditions. H-NS, a nucleoid protein, is known as a DNA-binding protein involved in bgl silencing. However, we previously found that bgl expression is still silent in a certain subset of hns mutations, each of which results in a defect...
Topics
- Bacterial Proteins
- DNA-Binding Proteins
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Gene Silencing
- Glucosides
- Molecular Chaperones
- Mutation
- Operon
- Peptide Fragments
