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
言語種別 英語
発行・発表の年月 2009/08
形態種別 研究論文
査読 査読あり
標題 Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space
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 106(34),pp.14403-14407
著者・共著者 Shin Kawano,Koji Yamano,Mari Naoe,Takaki Momose,Kayoko Terao,Shuh-ichi Nishikawa,Nobuhisa Watanabe,Toshiya Endo
概要 The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding require recognition and disulfide bond transfer by an oxidative translocator Tim40/Mia40 in the inner membrane facing the IMS. Here we determined the crystal structure of the core domain of yeast Mia40 (Mia40C4) as a fusion protein with maltose-binding protein at a resolution of 3 angstrom. The overall structure of Mia40C4 is a fruit-dish-like shape with a hydrophobic concave region, which accommodates a linker segment of the fusion protein in a helical conformation, likely mimicking a bound substrate. Replacement of the hydrophobic residues in this region resulted in growth defects and impaired assembly of a substrate protein. The Cys296-Cys298 disulfide bond is close to the hydrophobic concave region or possible substrate-binding site, so that it can mediate disulfide bond transfer to substrate proteins. These results are consistent with the growth phenotypes of Mia40 mutant cells containing Ser replacement of the conserved cysteine residues.
DOI 10.1073/pnas.0901793106
ISSN 0027-8424