新生多肽链在与分子伴侣形成的高分子质量组装体中的折叠。

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.

作者信息

Frydman J, Nimmesgern E, Ohtsuka K, Hartl F U

机构信息

Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

出版信息

Nature. 1994 Jul 14;370(6485):111-7. doi: 10.1038/370111a0.

DOI:10.1038/370111a0

PMID:8022479

Abstract

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.

摘要

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。