Recent advances in understanding catalysis of protein folding by molecular chaperones

Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress‐induced unfolding. A fundamental function of molecular ch...

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Published inFEBS letters Vol. 594; no. 17; pp. 2770 - 2781
Main Authors Balchin, David, Hayer‐Hartl, Manajit, Hartl, F. Ulrich
Format Journal Article
LanguageEnglish
Published England 01.09.2020
Subjects
catalytic activity
chaperonin
chaperonins
confinement
DnaK
GroEL
Hsp40
Hsp60
Hsp70
hydrophobicity
molecular chaperones
protein folding
protein misfolding
Hsp70
Hsp60
DnaK
confinement
GroEL
chaperonin
protein misfolding
protein folding
molecular chaperones
Hsp40
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Summary:Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress‐induced unfolding. A fundamental function of molecular chaperones is to inhibit unproductive protein interactions by recognizing and protecting hydrophobic surfaces that are exposed during folding or following proteotoxic stress. Beyond this basic principle, it is now clear that chaperones can also actively and specifically accelerate folding reactions in an ATP‐dependent manner. We focus on the bacterial Hsp70 and chaperonin systems as paradigms, and review recent work that has advanced our understanding of how these chaperones act as catalysts of protein folding.
Bibliography:Edited by Miguel De la Rosa
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ISSN:0014-5793
1873-3468
1873-3468
DOI:10.1002/1873-3468.13844