Stolz J, Sauer N (1999)
Publication Language: English
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 1999
Book Volume: 274
Pages Range: 18747-18752
Journal Issue: 26
Open Access Link: http://www.jbc.org/content/274/26/18747.long
The product of the FEN2 gene of Saccharomyces cerevisiae has previously been described as a protein conferring sensitivity to the antifungal agent fenpropimorph. Fen2p was postulated to act as a common regulator of carbon and nitrogen catabolite repression and of amino acid and ergosterol biosynthesis. In this paper, we present experimental evidence characterizing Fen2p as a plasma membrane-localized transporter for the vitamin pantothenate. The high affinity transport system (Km = 3.5 microM) is sensitive to uncouplers, suggesting a H+-pantothenate cotransport. Pantothenate transport rates in yeast are modulated by extracellular pantothenate, being maximal at low pantothenate concentrations. It is demonstrated that beta-alanine can suppress the growth defect of FEN2 wild-type and fen2 mutant cells on pantothenate-free medium. Evidence is presented that beta-alanine is transported by the general amino acid permease Gap1p. The relation among pantothenate transport, nitrogen catabolite repression, and sensitivity to the antifungal agent fenpropimorph is discussed.
APA:
Stolz, J., & Sauer, N. (1999). The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae encodes a plasma membrane H+-pantothenate symporter. Journal of Biological Chemistry, 274(26), 18747-18752. https://doi.org/10.1074/jbc.274.26.18747
MLA:
Stolz, Jürgen, and Norbert Sauer. "The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae encodes a plasma membrane H+-pantothenate symporter." Journal of Biological Chemistry 274.26 (1999): 18747-18752.
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