Structural Basis for Protein Translocation by the Translocase of the Outer Mitochondrial Membrane
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- ARAISO Yuhei
- Department of Clinical Laboratory Science, Division of Health Sciences, Graduate School of Medical Science, Kanazawa University
Bibliographic Information
- Other Title
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- ミトコンドリアタンパク質搬入ゲートTOM複合体の立体構造
- ミトコンドリアタンパクシツ ハンニュウ ゲート TOM フクゴウタイ ノ リッタイ コウゾウ
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Abstract
<p>The TOM complex is the main entry gate for mitochondrial proteins. Recently we determined the Cryo-EM structure of the yeast TOM complex at 3.8 Å resolution. The structure shows the dimeric form consisting of two Tom40 β-barrel channels and α-helical transmembrane subunits. The structure-based biochemical analysis revealed that presequence-containing preproteins pass through the Tom40 channel in the middle of the dimer and are transferred to the TIM23 complex. On the other hand, presequence-less preproteins leave the channel at the periphery of the TOM complex and are relayed to the chaperone proteins. Our results demonstrate the efficient transfer mechanism of preproteins.</p>
Journal
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- Seibutsu Butsuri
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Seibutsu Butsuri 60 (5), 280-283, 2020
The Biophysical Society of Japan General Incorporated Association
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Details 詳細情報について
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- CRID
- 1390848647559348480
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- NII Article ID
- 130007919208
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- NII Book ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL BIB ID
- 030695418
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed