Laboratory of Molecular Physiology and Genetics, Department of Bioscience, Graduate School of Agriculture, Ehime University, 3-5-7 Tarumi, Matsuyama, Ehime 790-8566, Japan; Advanced Research Support Center (ADRES), Ehime University, 3-5-7 Tarumi, Matsuyama, Ehime 790-8566, Japan; Division of Cell-Free Life Science, Proteo-Science Center, Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
Laboratory of Molecular Physiology and Genetics, Department of Bioscience, Graduate School of Agriculture, Ehime University, 3-5-7 Tarumi, Matsuyama, Ehime 790-8566, Japan.
Biochim Biophys Acta Biomembr. 2021 Feb 1;1863(2):183507. doi: 10.1016/j.bbamem.2020.183507. Epub 2020 Nov 12.
The stm1 (SPAC17C9.10) gene of Schizosaccharomyces pombe is closely related to genes encoding vacuolar PQ-loop proteins, Ypq1, Ypq2, and Ypq3, of Saccharomyces cerevisiae. When stm1 fused with GFP was expressed in fission or budding yeast, Stm1-GFP localized at the vacuolar membrane. Isolated vacuolar membrane vesicles from S. cerevisiae cells overexpressing stm1 exhibited stm1-dependent arginine and lysine uptake activity. Exchange activity of arginine and histidine/arginine, as observed for Ypq2 of S. cerevisiae, was also detected in the vesicles expressing stm1. The expression levels of stm1 in S. pombe cells significantly affected the vacuolar contents of lysine, histidine, and arginine. These results suggest that Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids across the vacuolar membrane.
裂殖酵母的 stm1(SPAC17C9.10)基因与编码酵母液泡 PQ-环蛋白 Ypq1、Ypq2 和 Ypq3 的基因密切相关。当将 stm1 与 GFP 融合表达在裂殖酵母或芽殖酵母中时,Stm1-GFP 定位于液泡膜上。从过表达 stm1 的酵母细胞中分离的液泡膜小泡表现出依赖于 stm1 的精氨酸和赖氨酸摄取活性。在表达 stm1 的小泡中还检测到了类似于酵母 Ypq2 的精氨酸和组氨酸/精氨酸的交换活性。在 S. 裂殖酵母细胞中,stm1 的表达水平显著影响赖氨酸、组氨酸和精氨酸的液泡含量。这些结果表明 Stm1 是一种液泡 PQ-环蛋白,参与了碱性氨基酸穿过液泡膜的运输。