TY - JOUR
T1 - Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe
AU - Kawano-Kawada, Miyuki
AU - Ueda, Taisuke
AU - Mori, Hikari
AU - Ichimura, Haruka
AU - Takegawa, Kaoru
AU - Sekito, Takayuki
N1 - Funding Information:
We report grants from JSPS KAKENHI 18K05440, grants from JSPS KAKENHI 18K05560, grants from Toyo Institute of Food Technology, during the conduct of the study.Funding: This work was supported in part by JSPS KAKENHI (grant numbers 18K05440 to M. K.-K. and 18K05560 to T.S.), and a grant from the Toyo Institute of Food Technology, Hyogo, Japan (to M.K.-K). The determination of amino acid contents was carried out on a L-8900 at the Division of Genetic Research, the Advanced Research Support Center (ADRES), Ehime University.
Publisher Copyright:
© 2020 Elsevier B.V.
PY - 2021/2/1
Y1 - 2021/2/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbamem.2020.183507
DO - 10.1016/j.bbamem.2020.183507
M3 - Article
C2 - 33189720
AN - SCOPUS:85096127698
SN - 0005-2736
VL - 1863
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 2
M1 - 183507
ER -