Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe

被引:1
作者
Kawano-Kawada, Miyuki [1 ,2 ,3 ]
Ueda, Taisuke [1 ]
Mori, Hikari [4 ]
Ichimura, Haruka [1 ]
Takegawa, Kaoru [4 ]
Sekito, Takayuki [1 ,3 ]
机构
[1] Ehime Univ, Grad Sch Agr, Dept Biosci, Lab Mol Physiol & Genet, 3-5-7 Tarumi, Matsuyama, Ehime 7908566, Japan
[2] Ehime Univ, Adv Res Support Ctr ADRES, 3-5-7 Tarumi, Matsuyama, Ehime 7908566, Japan
[3] Ehime Univ, Proteo Sci Ctr, Div Cell Free Life Sci, 3 Bunkyo Cho, Matsuyama, Ehime 7908577, Japan
[4] Kyushu Univ, Fac Agr, Dept Biosci & Biotechnol, Lab Appl Microbiol,Nishi Ku, 744 Motooka, Fukuoka 8190395, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2021年 / 1863卷 / 02期
关键词
Vacuolar membrane protein; Basic amino acids; Transport; PQ-loop; MEMBRANE-VESICLES; FAMILY; EXPRESSION; EXPORTER; VECTORS; GENE;
D O I
10.1016/j.bbamem.2020.183507
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 sttn1(+) 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.
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页数:9
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