期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 1, 页码 91-96出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1014918108
关键词
yeast; Tim50; Tom22
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Science and Technology Corporation
- National Institutes of Health [R01-GM54021, 5T32GM07445]
- Grants-in-Aid for Scientific Research [19058005] Funding Source: KAKEN
Mitochondria import most of their resident proteins from the cytosol, and the import receptor Tom20 of the outer-membrane translocator TOM40 complex plays an essential role in specificity of mitochondrial protein import. Here we analyzed the effects of Tom20 binding on NMR spectra of a long mitochondrial presequence and found that it contains two distinct Tom20-binding elements. In vitro import and cross-linking experiments revealed that, although the N-terminal Tom20-binding element is essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency.
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