Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
- 1 July 1994
- journal article
- Published by Springer Nature in Nature
- Vol. 370 (6485) , 111-117
- https://doi.org/10.1038/370111a0
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.Keywords
This publication has 52 references indexed in Scilit:
- Roles of molecular chaperones in protein foldingCurrent Opinion in Structural Biology, 1994
- Molecular chaperones in protein folding: the art of avoiding sticky situationsTrends in Biochemical Sciences, 1994
- Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiPCell, 1993
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Protein folding in the cellNature, 1992
- Peptide-binding specificity of the molecular chaperone BiPNature, 1991
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Peptide Binding and Release by Proteins Implicated as Catalysts of Protein AssemblyScience, 1989
- Coming in from the coldNature, 1988
- Proteins as molecular chaperonesNature, 1987