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Recent advances in understanding catalysis of protein folding by molecular chaperones
Author(s) -
Balchin David,
HayerHartl Manajit,
Hartl F. Ulrich
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13844
Subject(s) - co chaperone , chaperonin , protein folding , chaperone (clinical) , chemical chaperone , folding (dsp implementation) , chemistry , microbiology and biotechnology , foldase , hsp70 , unfolded protein response , biochemistry , biophysics , biology , heat shock protein , groel , computational biology , endoplasmic reticulum , escherichia coli , medicine , pathology , electrical engineering , gene , engineering
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.