Send to

Choose Destination
Nature. 1994 Jul 14;370(6485):111-7.

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

Author information

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


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.

Comment in

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center