Regulated expression of a repressor protein: FadR activates iclR
| Autor: | Alden Sunnarborg, David C. LaPorte, Lizhen Gui |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
DNA
Bacterial Operon Molecular Sequence Data lac operon Repressor Biology medicine.disease_cause Microbiology Bacterial Proteins Escherichia coli medicine Binding site Molecular Biology Gene Transcription factor Binding Sites Base Sequence Escherichia coli Proteins Glyoxylates Gene Expression Regulation Bacterial Carbon Repressor Proteins A-site Biochemistry Genes Bacterial DNA Probes Transcription Factors Research Article |
| Zdroj: | Journal of Bacteriology. 178:4704-4709 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.178.15.4704-4709.1996 |
| Popis: | The control of the glyoxylate bypass operon (aceBAK) of Escherichia coli is mediated by two regulatory proteins, IclMR and FadR. IclMR is a repressor protein which has previously been shown to bind to a site which overlaps the aceBAK promoter. FAR is a repressor/activator protein which participates in control of the genes of fatty acid metabolism. A sequence just upstream of the iclR promoter bears a striking resemblance to FadR binding sites found in the fatty acid metabolic genes. The in vitro binding specificity of FadR, determined by oligonucleotide selection, was in good agreement with the sequences of these sites. The ability of FadR to bind to the site associated with iclR was demonstrated by gel shift and DNase I footprint analyses. Disruption of FadR or inactivation of the FadR binding site of iclR decreased the expression of an iclR::lacZ operon fusion, indicating that FadR activates the expression of iclR. It has been reported that disruption of fadR increases the expression of aceBAK. We observed a similar increase when we inactivated the FadR binding site of an iclR+ allele. This result suggests that FadR regulates aceBAK indirectly by altering the expression of IclR. |
| Databáze: | OpenAIRE |
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