Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria

Hayashi Yamamoto, Nobuka Itoh, Shin Kawano, Yoh Ichi Yatsukawa, Takaki Momose, Tadashi Makio, Mayumi Matsunaga, Mihoko Yokota, Masatoshi Esaki, Toshihiro Shodai, Daisuke Kohda, Alyson E. Aiken Hobbs, Robert E. Jensen, Toshiya Endo

    Research output: Contribution to journalArticlepeer-review

    77 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)91-96
    Number of pages6
    JournalProceedings of the National Academy of Sciences of the United States of America
    Issue number1
    Publication statusPublished - Jan 4 2011

    All Science Journal Classification (ASJC) codes

    • General


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