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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 | 2012/10 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
| 執筆形態 | その他 |
| 掲載誌名 | MOLECULAR BIOLOGY OF THE CELL |
| 出版社・発行元 | AMER SOC CELL BIOLOGY |
| 巻・号・頁 | 23(20),pp.3936-3947 |
| 著者・共著者 | Takuya Shiota,Miyuki Maruyama,Mami Miura,Yasushi Tamura,Koji Yamano,Masatoshi Esaki,Toshiya Endo |
| 概要 | The TOM40 complex is a protein translocator in the mitochondrial outer membrane and consists of several different subunits. Among them, Tom40 is a central subunit that constitutes a protein-conducting channel by forming a beta-barrel structure. To probe the nature of the assembly process of Tom40 in the outer membrane, we attached various mitochondrial presequences to Tom40 that possess sorting information for the intermembrane space (IMS), inner membrane, and matrix and would compete with the inherent Tom40 assembly process. We analyzed the mitochondrial import of those fusion proteins in vitro. Tom40 crossed the outer membrane and/or inner membrane even in the presence of various sorting signals. N-terminal anchorage of the attached presequence to the inner membrane did not prevent Tom40 from associating with the TOB/SAM complex, although it impaired its efficient release from the TOB complex in vitro but not in vivo. The IMS or matrix-targeting presequence attached to Tom40 was effective in substituting for the requirement for small Tim proteins in the IMS for the translocation of Tom40 across the outer membrane. These results provide insight into the mechanism responsible for the precise delivery of beta-barrel proteins to the outer mitochondrial membrane. |
| DOI | 10.1091/mbc.E12-03-0202 |
| ISSN | 1059-1524 |