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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 1995/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Mitochondrial receptor complex protein - The intermembrane space domain of yeast MAS17 is not essential for its targeting or function |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BIOLOGICAL CHEMISTRY |
| 出版社・発行元 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 巻・号・頁 | 270(51),pp.30571-30575 |
| 著者・共著者 | M Nakai,K Kinoshita,T Endo |
| 概要 | MAS17 (MAS22) is an essential component of the import receptor complex in the yeast mitochondrial outer membrane. MAS17 consists of three distinct domains: the N-terminal cytosolic domain, the internal membrane-spanning domain, and the C-terminal intermembrane space domain. In the present study, we examined the roles of the C-terminal domain of MAS17, which is rich in acidic amino acids, in protein import into mitochondria both in vivo and in vitro. Cells expressing MAS17 Delta 120-152, a mutant MAS17 lacking the C-terminal acidic domain, could grow as fast as those expressing wild-type MAS17, while cells expressing MAS17 Delta 97-152, a mutant MAS17 lacking both the intermembrane space and the membrane-spanning domains, stopped growing as soon as wild-type MAS17 was depleted. MAS17 Delta 120-152 was correctly integrated into the mitochondrial outer membrane like wild-type MAS17. Mitochondria containing MAS17 Delta 120-152 instead of wildtype MAS17 could import both authentic and artificial mitochondrial precursor proteins nearly as efficiently as wild-type mitochondria in vitro. These results suggest that the C-terminal intermembrane space domain of MAS17 is not essential for targeting or functions of MAS17. |
| ISSN | 0021-9258 |