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  • Short Communication
  • Open Access

Brefeldin a decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae

  • 1,
  • 1,
  • 1,
  • 1,
  • 2 and
  • 1Email author
Cellular & Molecular Biology LettersAn International Journal200611:20

https://doi.org/10.2478/s11658-006-0020-8

  • Received: 4 January 2006
  • Accepted: 20 March 2006
  • Published:

Abstract

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.

Key words

  • Brefeldin A
  • Leucine permeases
  • Saccharomyces cerevisiae

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