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线粒体膜外进口复合物的功能可交换的独立进化。

Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes.

机构信息

Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.

Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.

出版信息

Elife. 2018 Jun 20;7:e34488. doi: 10.7554/eLife.34488.

DOI:10.7554/eLife.34488
PMID:29923829
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6010339/
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.

摘要

线粒体外膜（MOM）蛋白亚基的组装和/或插入，包括主要 MOM 易位酶的亚基，需要真菌特异性的 Mim1/Mim2 复合物。到目前为止，尚不清楚其他真核生物中的哪些蛋白质完成了这项任务。在这里，我们通过相互互补证明了原生动物的 MOM 蛋白 pATOM36 是酵母 Mim1/Mim2 复合物的功能类似物，尽管这些蛋白质既没有序列也没有拓扑相似性。pATOM36 的表达挽救了酵母细胞中缺乏 Mim1 和/或 Mim2 的几乎所有生长、线粒体生物发生和形态缺陷。相反，Mim1 和 Mim2 的共表达恢复了 pATOM36 缺失的原生动物中 MOM 蛋白的组装和/或插入缺陷。Mim1/Mim2 和 pATOM36 在异源表达时形成类似天然的复合物，表明这些结构不包含其他蛋白质。我们的研究结果表明，Mim1/Mim2 和 pATOM36 是趋同进化的产物，仅在真菌和原生动物的祖先分化后才出现。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/6010339/0397993627fa/elife-34488-fig8-figsupp1.jpg
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