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
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
收藏
页码:111 / 117
页数:7
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