Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes

  • Daniela G Vitali
    Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany
  • Sandro Käser
    Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
  • Antonia Kolb
    Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany
  • Kai S Dimmer
    Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany
  • Andre Schneider
    Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
  • Doron Rapaport
    Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany

抄録

<jats:p>Assembly and/or insertion of a subset of mitochondrial outer membrane (MOM) proteins, including subunits of the main MOM translocase, require the fungi-specific Mim1/Mim2 complex. So far it was unclear which proteins accomplish this task in other eukaryotes. Here, we show by reciprocal complementation that the MOM protein pATOM36 of trypanosomes is a functional analogue of yeast Mim1/Mim2 complex, even though these proteins show neither sequence nor topological similarity. Expression of pATOM36 rescues almost all growth, mitochondrial biogenesis, and morphology defects in yeast cells lacking Mim1 and/or Mim2. Conversely, co-expression of Mim1 and Mim2 restores the assembly and/or insertion defects of MOM proteins in trypanosomes ablated for pATOM36. Mim1/Mim2 and pATOM36 form native-like complexes when heterologously expressed, indicating that additional proteins are not part of these structures. Our findings indicate that Mim1/Mim2 and pATOM36 are the products of convergent evolution and arose only after the ancestors of fungi and trypanosomatids diverged.</jats:p>

収録刊行物

  • eLife

    eLife 7 2018-06-20

    eLife Sciences Publications, Ltd

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