Brefeldin A decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae
| Autor: | Carlos A. Stella, Manuel Alonso, Vanesa G. Pannunzio, James R. Mattoon, Hilda I. Burgos, Andrea Monti Hughes |
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| Rok vydání: | 2006 |
| Předmět: |
Antifungal Agents
Saccharomyces cerevisiae Proteins Amino Acid Transport Systems Short Communication Mutant Saccharomyces cerevisiae Biochemistry symbols.namesake chemistry.chemical_compound Leucine Leucine permeases Molecular Biology Brefeldin A biology Permease Endoplasmic reticulum Cell Biology Golgi apparatus biology.organism_classification Transport protein Amino acid permease Kinetics chemistry symbols Citrulline Protons |
| Zdroj: | Cellular & Molecular Biology Letters |
| ISSN: | 1689-1392 |
| Popis: | Brefeldin A is a commonly used antifungal agent that reversibly blocks protein transport from the endoplasmic reticulum to the Golgi complex. In this study, we aimed to characterize L-leucine uptake in Saccharomyces cerevisiae in the presence of brefeldin A. For this purpose, we used a synthetic medium, containing L-proline and the detergent SDS, which allows the agent to permeate into the yeast cell. The results obtained with a wild type strain and a gap1 mutant indicate that BFA causes either direct or indirect modification of the transport and/or processing of L-leucine permeases. The presence of BFA affects the kinetic parameter values for L-leucine uptake and decreases not only the uptake mediated by the general system (GAP1), but also that through the specific BAP2 (S1) and/or S2 systems. |
| Databáze: | OpenAIRE |
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