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Mitochondrial protein import receptors in Kinetoplastids reveal convergent evolution over large phylogenetic distances

机译:运动质体中的线粒体蛋白输入受体揭示了在较大的系统发育距离上的趋同进化

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Mitochondrial protein import is essential for all eukaryotes and mediated by hetero-oligomeric protein translocases thought to be conserved within all eukaryotes. We have identified and analysed the function and architecture of the non-conventional outer membrane (OM) protein translocase in the early diverging eukaryote Trypanosoma brucei . It consists of six subunits that show no obvious homology to translocase components of other species. Two subunits are import receptors that have a unique topology and unique protein domains and thus evolved independently of the prototype receptors Tom20 and Tom70 . Our study suggests that protein import receptors were recruited to the core of the OM translocase after the divergence of the major eukaryotic supergroups. Moreover, it links the evolutionary history of mitochondrial protein import receptors to the origin of the eukaryotic supergroups.
机译:线粒体蛋白的导入对于所有真核生物都是必不可少的,并由认为在所有真核生物中均保守的异寡聚蛋白转位酶介导。我们已经确定并分析了非常规外膜(OM)蛋白易位酶在早发真核锥虫Trypanosoma brucei中的功能和结构。它由六个亚基组成,这些亚基与其他物种的转位酶组分没有明显的同源性。两个亚基是输入受体,具有独特的拓扑结构和独特的蛋白质结构域,因此独立于原型受体Tom20和Tom70进化。我们的研究表明,在主要的真核超群分化之后,蛋白质输入受体被募集到OM移位酶的核心。此外,它将线粒体蛋白输入受体的进化历史与真核超群的起源联系起来。

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