Combined, Functional Genomic-Biochemical Approach to Intermediary Metabolism: Interaction of Acivicin, a Glutamine Amidotransferase Inhibitor, with Escherichia coli K-12
| Autor: | Tina K. Van Dyk, Lixuan L. Huang, Mary Jane G. Reeve, Amy Cheng Vollmer, Michael P. Mccluskey, Dana R. Smulski, Robert A. LaRossa |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Glutamine
Nitrogenous Group Transferases Genetics and Molecular Biology Biology medicine.disease_cause Binding Competitive Microbiology Glutamine transport chemistry.chemical_compound Bacterial Proteins Aminohydrolases Escherichia coli medicine Enzyme Inhibitors Molecular Biology Acivicin Transaminases Histidine Anthranilate Synthase Glutamine amidotransferase chemistry.chemical_classification Gene Expression Profiling Imidazoles Isoxazoles Ribonucleotides Molecular biology Culture Media Enzyme Glutamine Amidotransferase Inhibitor chemistry Biochemistry |
| Zdroj: | Journal of Bacteriology. 183:3353-3364 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.183.11.3353-3364.2001 |
| Popis: | Acivicin, a modified amino acid natural product, is a glutamine analog. Thus, it might interfere with metabolism by hindering glutamine transport, formation, or usage in processes such as transamidation and translation. This molecule prevented the growth of Escherichia coli in minimal medium unless the medium was supplemented with a purine or histidine, suggesting that the HisHF enzyme, a glutamine amidotransferase, was the target of acivicin action. This enzyme, purified from E. coli , was inhibited by low concentrations of acivicin. Acivicin inhibition was overcome by the presence of three distinct genetic regions when harbored on multicopy plasmids. Comprehensive transcript profiling using DNA microarrays indicated that histidine biosynthesis was the predominant process blocked by acivicin. The response to acivicin, however, was quite complex, suggesting that acivicin inhibition resonated through more than a single cellular process. |
| Databáze: | OpenAIRE |
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