Resistance to trifluoroperazine, a calmodulin inhibitor, maps to the fabD locus in Escherichia coli
| Autor: | Tempête M, S. J. Séror, Bouquin N, I. B. Holland |
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| Rok vydání: | 1995 |
| Předmět: |
Cell division
Calmodulin Mutant Molecular Sequence Data medicine.disease_cause Bacterial Proteins Genetics medicine Acyl-Carrier Protein S-Malonyltransferase Escherichia coli Fatty Acid Synthase Type II Cloning Molecular Molecular Biology Gene chemistry.chemical_classification biology Base Sequence Escherichia coli Proteins Cell Membrane Fatty Acids Genetic Complementation Test Temperature Chromosome Mapping Drug Resistance Microbial Sequence Analysis DNA Molecular biology Trifluoperazine Complementation Molecular Weight Enzyme Subcloning Biochemistry chemistry Genes Bacterial Mutation biology.protein Acyltransferases |
| Zdroj: | Moleculargeneral genetics : MGG. 246(5) |
| ISSN: | 0026-8925 |
| Popis: | A mutant, tfpA1, resistant to the calmodulin inhibitor trifluoroperazine (TFP) at 30 degrees C, was isolated in Escherichia coli. The mutant showed a reduced growth rate at 30 degrees C and was temperature sensitive (ts) at 42 degrees C for growth, forming short filaments. The mutation was mapped to the 24 min region of the chromosome and the gene was cloned by complementation of the ts defect. Subsequent subcloning, complementation analysis, marker rescue mapping and sequencing, identified tfpA as fabD, encoding the 35 kDa, malonyl-coenzyme A transacylase (MCT) enzyme, required for the initial step in the elongation cycle for fatty acid biosynthesis. Resistance to TFP may result from altered permeability of the cell envelope, although the mutant remained sensitive to other calmodulin inhibitors and to other antibacterial agents. Alternatively, resistance may be more indirect, resulting from alterations in intracellular Ca++ levels which affect the activity of the TFP target in some way. |
| Databáze: | OpenAIRE |
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