Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes

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

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Käser, Sandro and Schneider, André

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

2050-084X

Publisher:

eLife Sciences Publications

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

30 Oct 2018 15:22

Last Modified:

23 Oct 2019 11:46

Publisher DOI:

10.7554/eLife.34488

PubMed ID:

29923829

BORIS DOI:

10.7892/boris.120721

URI:

https://boris.unibe.ch/id/eprint/120721

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