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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 | 2005/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements |
| 執筆形態 | その他 |
| 掲載誌名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
| 出版社・発行元 | NATL ACAD SCIENCES |
| 巻・号・頁 | 102(50),pp.17999-18004 |
| 著者・共著者 | T Sato,M Esaki,JM Fernandez,T Endo |
| 概要 | Many newly synthesized proteins have to become unfolded during translocation across biological membranes. We have analyzed the effects of various stabilization/destabilization mutations in the Ig-like module of the muscle protein titin upon its import from the IN terminus or C terminus into mitochondria. The effects of mutations on the import of the titin module from the C terminus correlate well with those on forced mechanical unfolding in atomic-force microscopy (AFM) measurements. On the other hand, as long as turnover of the mitochondrial Hsp70 system is not rate-limiting for the import, import of the titin module from the N terminus is sensitive to mutations in the N-terminal region but not the ones in the C-terminal region that affect resistance to global unfolding in AFM experiments. We propose that the mitochondrial-import system can catalyze precursor-unfolding by reducing the stability of unfolding intermediates. |
| DOI | 10.1073/pnas.0504495102 |
| ISSN | 0027-8424 |