PMID:9473058
| Citation |
Free, A, Williams, RM and Dorman, CJ (1998) The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli. J. Bacteriol. 180:994-7 |
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| 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. |
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| Keywords |
Amino Acid Transport Systems; Bacterial Proteins/biosynthesis; Carrier Proteins/biosynthesis; DNA-Binding Proteins/genetics; Enzyme Repression; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Reporter; Glucosides/metabolism; Molecular Chaperones; Mutation; Operon; Peptide Fragments/genetics; Sequence Deletion |
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