2020 Fiscal Year Final Research Report
Characterization of PQ-loop proteins involved in the vacuolar amino acid compartmentalization in yeasts
Project/Area Number |
18K05440
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Review Section |
Basic Section 38030:Applied biochemistry-related
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Research Institution | Ehime University |
Principal Investigator |
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Project Period (FY) |
2018-04-01 – 2021-03-31
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Keywords | 酵母 / 液胞 / トランスポーター / アミノ酸 / PQ-loopタンパク質 |
Outline of Final Research Achievements |
In this study, we investigated the mechanism of amino acid transport by yeast vacuolar PQ-loop proteins and indicated that the exchange activity of arginine/histidine across the vacuolar membrane of Saccharomyces cerevisiae is dependent on Ypq2. Furthermore, we identified Stm1 of Schizosaccharomyces pombe as a novel vacuolar membrane protein involved in the transport of basic amino acids. From the results of amino acid determination of vacuolar fractions of the mutants disrupted genes encoding these PQ-loop proteins, it was suggested that these vacuolar PQ-loop proteins operate at the vacuolar membrane for the export of basic amino acids, especially arginine, from vacuoles.
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Free Research Field |
応用生物化学
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Academic Significance and Societal Importance of the Research Achievements |
酵母の液胞は細胞内遊離アミノ酸の巨大な貯蔵庫であり、液胞アミノ酸含量は細胞の総アミノ酸量を大きく左右する。液胞内外へのアミノ酸輸送に関わる輸送タンパク質群の全体像解明により、液胞膜を介したアミノ酸輸送のコントロールによる、アミノ酸を高度もしくは選択的に蓄積した有用酵母株の創製が期待できる。
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