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) |
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Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) |
UniBE Contributor: |
Käser, Sandro, 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: |
05 Dec 2022 15:18 |
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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