Reference: Vitali DG, et al. (2018) Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes. Elife 7

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Abstract


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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Vitali DG, Käser S, Kolb A, Dimmer KS, Schneider A, Rapaport D
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