FOLDING OF NASCENT POLYPEPTIDE-CHAINS IN A HIGH-MOLECULAR-MASS ASSEMBLY WITH MOLECULAR CHAPERONES

被引：575

作者：

FRYDMAN, J

NIMMESGERN, E

OHTSUKA, K

HARTL, FU

机构：

[1] MEM SLOAN KETTERING CANC CTR,HOWARD HUGHES MED INST,NEW YORK,NY 10021

[2] MEM SLOAN KETTERING CANC CTR,CELLULAR BIOCHEM & BIPHYS PROGRAM,NEW YORK,NY 10021

[3] AICHI CANC CTR,EXPTL RADIOL LAB,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN

来源：

NATURE | 1994年 / 370卷 / 6485期

关键词：

D O I：

10.1038/370111a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：111 / 117

页数：7

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