Human Mpp11 J protein: Ribosome-tethered molecular chaperones are ubiquitous
Human Mpp11 J protein: Ribosome-tethered molecular chaperones are ubiquitous
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DOI：
10.1126/science.1109247
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发表时间：
2005-05-13
期刊：
影响因子：
56.9
通讯作者：
Craig, EA
中科院分区：
文献类型：
--
作者：
Hundley, HA;Walter, W;Craig, EA
直接与核糖体相互作用的特化分子伴侣的存在在微生物中得到了很好的证实。这些蛋白质结合离开核糖体隧道的多肽，并在翻译和蛋白质折叠之间提供物理联系。我们报告说，核糖体相关的分子伴侣一直保持在整个真核生物的进化，如Mpp11，酵母核糖体相关的J蛋白左的人类直系同源物所示。当在酵母中表达时，Mpp11通过与多用途Hsp70 Ssa（哺乳动物Hsc70的同源物）合作而部分取代Zuo。我们建议，在后生动物，核糖体相关的Mpp11招聘的多功能可溶性Hsc70新生的多肽链，因为它们退出核糖体。
The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.