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Import of ribosomal proteins into yeast mitochondria

机译:将核糖体蛋白导入酵母线粒体

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摘要

Mitochondrial ribosomes of baker's yeast contain at least 78 protein subunits. All but one of these proteins are nuclear-encoded, synthesized on cytosolic ribosomes, and imported into the matrix for biogenesis. The import of matrix proteins typically relies on N-terminal mitochondrial targeting sequences that form positively charged amphipathic helices. Interestingly, the N-terminal regions of many ribosomal proteins do not closely match the characteristics of matrix targeting sequences, suggesting that the import processes of these proteins might deviate to some extent from the general import route. So far, the biogenesis of only two ribosomal proteins, Mrpl32 and Mrp10, was studied experimentally and indeed showed surprising differences to the import of other preproteins. In this review article we summarize the current knowledge on the transport of proteins into the mitochondrial matrix, and thereby specifically focus on proteins of the mitochondrial ribosome.
机译:面包酵母的线粒体核糖体含有至少78个蛋白质亚基。除一种蛋白质外,所有蛋白质都经过核编码,在胞质核糖体上合成,并导入基质中以进行生物发生。基质蛋白的导入通常依赖于N端线粒体靶向序列,该序列形成带正电的两亲螺旋。有趣的是,许多核糖体蛋白的N端区域与基质靶向序列的特征不完全匹配,这表明这些蛋白的导入过程可能在某种程度上偏离一般的导入途径。到目前为止,仅对两种核糖体蛋白Mrpl32和Mrp10的生物发生进行了实验研究,的确显示出与其他前蛋白的导入有惊人的差异。在这篇综述文章中,我们总结了蛋白质转运到线粒体基质中的当前知识,因此特别关注线粒体核糖体的蛋白质。

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