Import of ribosomal proteins into yeast mitochondria.

Import of ribosomal proteins into yeast mitochondria.
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将核糖体蛋白导入酵母线粒体

DOI:
10.1139/bcb-2014-0029
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发表时间:
2014
期刊:
Biochemistry and cell biology = Biochimie et biologie cellulaire
影响因子:
--
通讯作者:
Herrmann JM
Herrmann JM
中科院分区:
--
文献类型:
--
作者:
Woellhaf MW;Hansen KG;Garth C;Herrmann JM

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面包酵母的线粒体核糖体含有至少78个蛋白质亚基。这些蛋白质中除了一种以外都是核编码的,在胞质核糖体上合成,并输入到基质中进行生物合成。基质蛋白的输入通常依赖于形成带正电荷的两亲性螺旋的N-末端线粒体靶向序列。有趣的是,许多核糖体蛋白的N-末端区域与基质靶向序列的特征并不紧密匹配,这表明这些蛋白的输入过程可能在一定程度上偏离一般的输入途径。到目前为止,只有两个核糖体蛋白,Mrp 132和Mrp 10的生物发生进行了实验研究,并确实显示出令人惊讶的差异,其他前蛋白的输入。在这篇综述文章中,我们总结了目前的知识转运蛋白质进入线粒体基质,从而特别关注蛋白质的线粒体核糖体。
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.
DOI: 10.1038/86253
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