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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Chaperone receptors: Guiding proteins to intracellular compartments
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Chaperone receptors: Guiding proteins to intracellular compartments

机译：伴侣受体：指导蛋白质进入细胞内区室

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Despite mitochondria and chloroplasts having their own genome, 99% of mitochondrial proteins (Rehling et al., Nat Rev Mol Cell Biol 5:519-530, 2004) and more than 95% of chloroplast proteins (Soll, Curr Opin Plant Biol 5:529-535, 2002) are encoded by nuclear DNA, synthesised in the cytosol and imported post-translationally. Protein targeting to these organelles depends on cytosolic targeting factors, which bind to the precursor, and then interact with membrane receptors to deliver the precursor into a translocase. The molecular chaperones Hsp70 and Hsp90 have been widely implicated in protein targeting to mitochondria and chloroplasts, and receptors capable of recognising these chaperones have been identified at the surface of both these organelles (Schlegel et al., Mol Biol Evol 24:2763-2774, 2007). The role of these chaperone receptors is not fully understood, but they have been shown to increase the efficiency of protein targeting (Young et al., Cell 112:41-50, 2003; Qbadou et al., EMBO J 25:1836-1847, 2006). Whether these receptors contribute to the specificity of targeting is less clear. A class of chaperone receptors bearing tetratricopeptide repeat domains is able to specifically bind the highly conserved C terminus of Hsp70 and/or Hsp90. Interestingly, at least of one these chaperone receptors can be found on each organelle (Schlegel et al., Mol Biol Evol 24:2763-2774, 2007), which suggests a universal role in protein targeting for these chaperone receptors. This review will investigate the role that chaperone receptors play in targeting efficiency and specificity, as well as examining recent in silico approaches to find novel chaperone receptors.
机译：尽管线粒体和叶绿体具有自己的基因组，但99％的线粒体蛋白（Rehling等人，Nat Rev Mol Cell Biol 5：519-530，2004）和95％以上的叶绿体蛋白（Soll，Curr Opin Plant Biol 5： 529-535，2002）由核DNA编码，在细胞质中合成并在翻译后导入。靶向这些细胞器的蛋白质取决于胞质靶向因子，该因子与前体结合，然后与膜受体相互作用，将前体递送到转位酶中。分子伴侣蛋白Hsp70和Hsp90已广泛参与靶向线粒体和叶绿体的蛋白质，并且在这两个细胞器的表面均已鉴定出能够识别这些分子伴侣的受体（Schlegel等，Mol Biol Evol 24：2763-2774， 2007）。这些伴侣受体的作用尚不完全清楚，但已显示它们可提高蛋白质靶向的效率（Young等人，Cell 112：41-50，2003; Qbadou等人，EMBO J 25：1836-1847 ，2006）。这些受体是否有助于靶向特异性尚不清楚。一类带有四三肽重复结构域的伴侣受体能够特异性结合Hsp70和/或Hsp90的高度保守的C末端。有趣的是，这些伴侣蛋白受体中的至少一种可以在每个细胞器上找到（Schlegel等人，Mol Biol Evol 24：2763-2774，2007），这暗示了在针对这些伴侣蛋白的蛋白质靶向中的普遍作用。这篇综述将调查伴侣蛋白受体在靶向效率和特异性中的作用，并研究最近的计算机方法以发现新型伴侣蛋白受体。

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