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Evolutionary conservation of biogenesis of β-barrel membrane proteins

机译：β-桶状膜蛋白生物发生的进化保守性

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摘要

The outer membranes of mitochondria and chloroplasts are distinguished by the presence of β-barrel membrane proteins, The outer membrane of Gram-negative bacteria also harbours β-barrel proteins. In mitochondria these proteins fulfil a variety of functions such as transport of small molecules (porin/VDAC), translocation of proteins (Tom40) and regulation of mitochondrial morphology (Mdm10). These proteins are encoded by the nucleus, synthesized in the cytosol, targeted to mitochondria as chaperone-bound species, recognized by the translocase of the outer membrane, and then inserted into the outer membrane where they assemble into functional oligomers. Whereas some knowledge has been accumulated on the pathways of insertion of proteins that span cellular membranes with α-helical segments, very little is known about how β-barrel proteins are integrated into lipid bilayers and assembled into oligomeric structures. Here we describe a protein complex that is essential for the topogenesis of mitochondrial outer membrane β-barrel proteins (TOB). We present evidence that important elements of the topogenesis of β-barrel membrane proteins have been conserved during the evolution of mitochondria from endosymbiotic bacterial ancestors.
机译：线粒体和叶绿体的外膜以β-桶状膜蛋白的存在为特征。革兰氏阴性细菌的外膜也带有β-桶状蛋白。在线粒体中，这些蛋白质具有多种功能，例如小分子的运输（孔蛋白/ VDAC），蛋白质的转运（Tom40）和线粒体形态的调控（Mdm10）。这些蛋白质由细胞核中的核编码，在细胞质中合成，靶向与伴侣结合的线粒体，被外膜的转座酶识别，然后插入外膜，在那里它们组装成功能性低聚物。尽管已经积累了跨越具有α-螺旋节段的细胞膜的蛋白质的插入途径的一些知识，但对于β-桶状蛋白质如何整合到脂质双层中并组装成寡聚结构的了解却很少。在这里，我们描述了一种蛋白质复合物，它对于线粒体外膜β-桶状蛋白质（TOB）的拓扑生成至关重要。我们提供的证据表明，从内共生细菌祖先的线粒体进化过程中，β-桶状膜蛋白的拓扑结构的重要组成部分已被保守。

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