Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20

Yoshito Abe, Toshihiro Shodai, Takanori Muto, Katsuyoshi Mihara, Hisayoshi Torii, Shuh ichi Nishikawa, Toshiya Endo, Daisuke Kohda

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361 Citations (Scopus)


Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all α-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.

Original languageEnglish
Pages (from-to)551-560
Number of pages10
Issue number5
Publication statusPublished - Mar 3 2000
Externally publishedYes


All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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