In nutrient-rich conditions, basic amino acids are actively accumulated into the vacuoles by H⁺-coupled transporters in Saccharomyces cerevisiae. In addition to the H⁺-coupled systems, the existence of an exchanger for arginine and histidine was indicated by kinetic analysis using isolated vacuolar membrane vesicles; however, the gene(s) involved in the activity has not been identified. Here, we show that the uptake activity of arginine driven by an artificially imposed histidine gradient decreased significantly by the disruption of the gene encoding vacuolar PQ-loop protein Ypq2, but not by those of Ypq1 and Ypq3. The exchange activity was restored by the expression of YPQ2. Furthermore, the substitution of a conserved proline residue, Pro29, in Ypq2 greatly decreased the exchange activity. These results suggest that Ypq2 is responsible for the exchange activity of arginine and histidine across the vacuolar membrane, and the conserved proline residue in the PQ-loop motif is required for the activity.

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Journal Article | Research Support, Non-U.S. Gov't

Authors

Kawano-Kawada M, Manabe K, Ichimura H, Kimura T, Harada Y, Ikeda K, Tanaka S, Kakinuma Y, Sekito T

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