Brefeldin A decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae.
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.
Alonso
Manuel
M
Department of Biochemistry, School of Medicine, University of Buenos Aires, Paraguay, Piso, Argentina.
Burgos
Hilda I
HI
Pannunzio
Vanesa
V
Monti Hughes
Andrea
A
Mattoon
James R
JR
Stella
Carlos A
CA
D026905:Amino Acid Transport Systems / Q000378:metabolism*; D000935:Antifungal Agents / Q000494:pharmacology*; D020126:Brefeldin A / Q000494:pharmacology*; D002956:Citrulline / Q000378:metabolism; D007700:Kinetics; D007930:Leucine / Q000378:metabolism*; D011522:Protons; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
D026905:Amino Acid Transport Systems; D000935:Antifungal Agents; C491145:GAP1 protein, S cerevisiae; D011522:Protons; D029701:Saccharomyces cerevisiae Proteins; D020126:Brefeldin A; D002956:Citrulline; D007930:Leucine