†Present address: Department of Cell and Molecular Biology/Microbiology, Göteborg University, Box 462, S-405 30 Göteborg, Sweden.
The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae
Article first published online: 21 DEC 2001
Volume 40, Issue 6, pages 1391–1401, June 2001
How to Cite
Wysocki, R., Chéry, C. C., Wawrzycka, D., Van Hulle, M., Cornelis, R., Thevelein, J. M. and Tamás, M. J. (2001), The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae. Molecular Microbiology, 40: 1391–1401. doi: 10.1046/j.1365-2958.2001.02485.x
- Issue published online: 21 DEC 2001
- Article first published online: 21 DEC 2001
- Accepted 12 April, 2001.
The Saccharomyces cerevisiae FPS1 gene encodes a glycerol channel protein involved in osmoregulation. We present evidence that Fps1p mediates influx of the trivalent metalloids arsenite and antimonite in yeast. Deletion of FPS1 improves tolerance to arsenite and potassium antimonyl tartrate. Under high osmolarity conditions, when the Fps1p channel is closed, wild-type cells show the same degree of As(III) and Sb(III) tolerance as the fps1Δ mutant. Additional deletion of FPS1 in mutants defective in arsenite and antimonite detoxification partially suppresses their hypersensitivity to metalloid salts. Cells expressing a constitutively open form of the Fps1p channel are highly sensitive to both arsenite and antimonite. We also show by direct transport assays that arsenite uptake is mediated by Fps1p. Yeast cells appear to control the Fps1p-mediated pathway of metalloid uptake, as expression of the FPS1 gene is repressed upon As(III) and Sb(III) addition. To our knowledge, this is the first report describing a eukaryotic uptake mechanism for arsenite and antimonite and its involvement in metalloid tolerance.