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Functional Expression ofSchizosaccharomyces pombeVba2p in the Vacuolar Membrane ofSaccharomyces cerevisiae
Author(s) -
Pongsanat Pongcharoen,
Miyuki KawanoKawada,
Tomoko Iwaki,
Naoko Sugimoto,
Takayuki Sekito,
Koichi Akiyama,
Kaoru Takegawa,
Yoshimi Kakinuma
Publication year - 2013
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.130387
Subject(s) - schizosaccharomyces pombe , saccharomyces cerevisiae , lysine , vacuole , yeast , quinidine , biochemistry , membrane , vesicle , schizosaccharomyces , chemistry , microbiology and biotechnology , amino acid , biology , cytoplasm , pharmacology
A vacuolar membrane protein, Vba2p of Schizosaccharomyces pombe, is involved in basic amino acid uptake by intact cells. Here we found evidence that Vba2p mediated ATP-dependent lysine uptake by vacuolar membrane vesicles of Saccharomyces cerevisiae. Vba2p was also responsible for quinidine sensitivity, and the addition of lysine improved cell growth on quinidine-containing media. These findings should be useful for further characterization of Vba2p.

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