Frydman J, Nimmesgern E, Ohtsuka K, Hartl F U
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
Nature. 1994 Jul 14;370(6485):111-7. doi: 10.1038/370111a0.
The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the chaperonin TRiC. The ordered assembly of these components on the nascent chain forms a high molecular mass complex that allows the cotranslational formation of protein domains and the completion of folding once the chain is released from the ribosome.
在哺乳动物翻译系统中，以萤火虫荧光素酶作为模型蛋白，对核糖体产生的多肽折叠进行了分析。正在生长的多肽与一组特定的分子伴侣相互作用，包括热休克蛋白70（Hsp70）、DnaJ同源物热休克蛋白40（Hsp40）和伴侣蛋白TRiC。这些组分在新生链上有序组装形成一个高分子量复合物，该复合物允许在翻译过程中形成蛋白质结构域，并在链从核糖体释放后完成折叠。
