Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes

Autor: Daniela G Vitali, Sandro Käser, Antonia Kolb, Kai S Dimmer, Andre Schneider, Doron Rapaport
Rok vydání: 2017
Předmět:
Zdroj: eLife, Vol 7 (2018)
Vitali, Daniela G; Käser, Sandro; Kolb, Antonia; Dimmer, Kai S; Schneider, André; Rapaport, Doron (2018). Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes. eLife, 7 eLife Sciences Publications 10.7554/eLife.34488
ISSN: 2050-084X
DOI: 10.7554/eLife.34488
Popis: 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.
Databáze: OpenAIRE