FOLDING OF NEWLY TRANSLATED PROTEINS IN VIVO: The Role of Molecular Chaperones

Recent years have witnessed dramatic advances in our understanding of how newly translated proteins fold in the cell and the contribution of molecular chaperones to this process. Folding in the cell must be achieved in a highly crowded macromolecular environment, in which release of nonnative polype...

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Bibliographic Details
Published in:Annual review of biochemistry 2001-01, Vol.70 (1), p.603-647
Main Author: Frydman, Judith
Format: Article
Language:English
Subjects:
Amino acids
Aqueous solutions
Biochemical analysis
Cell Compartmentation
chaperonin
cotranslational folding
Cytoplasm
Cytosol - metabolism
Eukaryotic Cells
GroEL
Hsp70
HSP70 Heat-Shock Proteins - metabolism
HSP90 Heat-Shock Proteins - metabolism
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Polypeptides
Protein Biosynthesis
Protein Folding
Protein Processing, Post-Translational
Protein Transport
Proteins
TRiC/CCT
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Summary:Recent years have witnessed dramatic advances in our understanding of how newly translated proteins fold in the cell and the contribution of molecular chaperones to this process. Folding in the cell must be achieved in a highly crowded macromolecular environment, in which release of nonnative polypeptides into the cytosolic solution might lead to formation of potentially toxic aggregates. Here I review the cellular mechanisms that ensure efficient folding of newly translated proteins in vivo. De novo protein folding appears to occur in a protected environment created by a highly processive chaperone machinery that is directly coupled to translation. Genetic and biochemical analysis shows that several distinct chaperone systems, including Hsp70 and the cylindrical chaperonins, assist the folding of proteins upon translation in the cytosol of both prokaryotic and eukaryotic cells. The cellular chaperone machinery is specifically recruited to bind to ribosomes and protects nascent chains and folding intermediates from nonproductive interactions. In addition, initiation of folding during translation appears to be important for efficient folding of multidomain proteins.
ISSN:0066-4154
1545-4509
DOI:10.1146/annurev.biochem.70.1.603