Abstract / Description of output
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 language | English |
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Pages (from-to) | 994-7 |
Number of pages | 4 |
Journal | Journal of Bacteriology |
Volume | 180 |
Issue number | 4 |
Publication status | Published - Feb 1998 |
Keywords / Materials (for Non-textual outputs)
- 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