Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
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DOI：
10.1126/science.272.5267.1497
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发表时间：
1996-06-07
期刊：
影响因子：
56.9
通讯作者：
Hartl, FU
中科院分区：
文献类型：
--
作者：
Frydman, J;Hartl, FU
真核细胞质溶胶中的分子伴侣与化学变性蛋白及其新翻译的对应物的相互作用不同。在复性过程中，从变性剂，肌动蛋白之间的70千道尔顿热休克蛋白，散装胞质溶胶，和伴侣蛋白TCP 1环复合物自由分配。相反，在无细胞翻译过程中，分子伴侣被募集到延伸多肽中，并保护其在折叠过程中免于暴露于大量胞质溶胶。在寡聚蛋白亚基和异常多肽中观察到分子伴侣结合和游离状态之间的翻译后循环;这种循环允许亚基组装和异常多肽降解。因此，折叠、寡聚化和降解在层次上相关联，以确保新合成的多肽的正确命运。
Molecular chaperones in the eukaryotic cytosol were shown to interact differently with chemically denatured proteins and their newly translated counterparts. During refolding from denaturant, actin partitioned freely between 70-kilodalton heat shock protein, the bulk cytosol, and the chaperonin TCP1-ring complex. In contrast, during cell-free translation, the chaperones were recruited to the elongating polypeptide and protected it from exposure to the bulk cytosol during folding. Posttranslational cycling between chaperone-bound and free states was observed with subunits of oligomeric proteins and with aberrant polypeptides; this cycling allowed the subunits to assemble and the aberrant polypeptides to be degraded. Thus, folding, oligomerization, and degradation are linked hierarchically to ensure the correct fate of newly synthesized polypeptides.