Agp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level

被引:27
作者
Aouida, Mustapha [1 ]
Texeira, Marta Rubio [2 ,3 ]
Thevelein, Johan M. [2 ,3 ]
Poulin, Richard [4 ]
Ramotar, Dindial [5 ]
机构
[1] King Abdullah Univ Sci & Technol, Ctr Desert Agr, Thuwal, Saudi Arabia
[2] Inst Bot & Microbiol, Mol Cell Biol Lab, Louvain, Belgium
[3] Flanders Inst Biotechnol, Dept Mol Microbiol, Flanders, Belgium
[4] Univ Laval, Dept Mol Biol Med Biochem & Pathol, Quebec City, PQ G1K 7P4, Canada
[5] Univ Montreal, Maisonneuve Rosemont Hosp, Res Ctr, Montreal, PQ, Canada
来源
PLOS ONE | 2013年 / 8卷 / 06期
关键词
SR PROTEIN-KINASE; SACCHAROMYCES-CEREVISIAE; POTASSIUM TRANSPORTER; ION HOMEOSTASIS; DRUG BLEOMYCIN; BUDDING YEAST; PATHWAY; GENE; ACTIVATION; TOLERANCE;
D O I
10.1371/journal.pone.0065717
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Agp2 is a plasma membrane protein of the Saccharomyces cerevisiae amino acid transporter family, involved in high-affinity uptake of various substrates including L-carnitine and polyamines. The discovery of two high affinity polyamine permeases, Dur3 and Sam3, prompted us to investigate whether Agp2 directly transports polyamines or acts instead as a regulator. Herein, we show that neither dur3 Delta nor sam3 Delta single mutant is defective in polyamine transport, while the dur3 Delta sam3 Delta double mutant exhibits a sharp decrease in polyamine uptake and an increased resistance to polyamine toxicity similar to the agp2 Delta mutant. Studies of Agp2 localization indicate that in the double mutant dur3 Delta sam3 Delta, Agp2-GFP remains plasma membrane-localized, even though transport of polyamines is strongly reduced. We further demonstrate that Agp2 controls the expression of several transporter genes including DUR3 and SAM3, the carnitine transporter HNM1 and several hexose, nucleoside and vitamin permease genes, in addition to SKY1 encoding a SR kinase that positively regulates low-affinity polyamine uptake. Furthermore, gene expression analysis clearly suggests that Agp2 is a strong positive regulator of additional biological processes. Collectively, our data suggest that Agp2 might respond to environmental cues and thus regulate the expression of several genes including those involved in polyamine transport.
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页数:14
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