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 | 2015/09 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Molecular architecture of the active mitochondrial protein gate |
執筆形態 | その他 |
掲載誌名 | SCIENCE |
出版社・発行元 | AMER ASSOC ADVANCEMENT SCIENCE |
巻・号・頁 | 349(6255),pp.1544-1548 |
著者・共著者 | Takuya Shiota,Kenichiro Imai,Jian Qiu,Victoria L. Hewitt,Khershing Tan,Hsin-Hui Shen,Noriyuki Sakiyama,Yoshinori Fukasawa,Sikander Hayat,Megumi Kamiya,Arne Elofsson,Kentaro Tomii,Paul Horton,Nils Wiedemann,Nikolaus Pfanner,Trevor Lithgow,Toshiya Endo |
概要 | Mitochondria fulfill central functions in cellular energetics, metabolism, and signaling. The outer membrane translocator complex (the TOM complex) imports most mitochondrial proteins, but its architecture is unknown. Using a cross-linking approach, we mapped the active translocator down to single amino acid residues, revealing different transport paths for preproteins through the Tom40 channel. An N-terminal segment of Tom40 passes from the cytosol through the channel to recruit chaperones fromthe intermembrane space that guide the transfer of hydrophobic preproteins. The translocator contains three Tom40 beta-barrel channels sandwiched between a central alpha-helical Tom22 receptor cluster and external regulatory Tom proteins. The preprotein-translocating trimeric complex exchanges with a dimeric isoform to assemble new TOM complexes. Dynamic coupling of alpha-helical receptors, beta-barrel channels, and chaperones generates a versatile machinery that transports about 1000 different proteins. |
DOI | 10.1126/science.aac6428 |
ISSN | 0036-8075/1095-9203 |
PMID | 26404837 |