Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 294, Issue 6, Pages 2085-2097Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.REV118.002810
Keywords
molecular chaperone; 70-kilodalton heat shock protein (Hsp70); protein folding; allosteric regulation; chaperone DnaK (DnaK); chaperone DnaJ (DnaJ); nanomachine; J-domain; protein homeostasis
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Funding
- NIGMS NIH HHS [R35 GM118161] Funding Source: Medline
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Hsp70 chaperones are central hubs of the protein quality control network and collaborate with co-chaperones having a J-domain (an approximate to 70-residue-long helical hairpin with a flexible loop and a conserved His-Pro-Asp motif required for ATP hydrolysis by Hsp70s) and also with nucleotide exchange factors to facilitate many protein-folding processes that (re)establish protein homeostasis. The Hsp70s are highly dynamic nanomachines that modulate the conformation of their substrate polypeptides by transiently binding to short, mostly hydrophobic stretches. This interaction is regulated by an intricate allosteric mechanism. The J-domain co-chaperones target Hsp70 to their polypeptide substrates, and the nucleotide exchange factors regulate the lifetime of the Hsp70-substrate complexes. Significant advances in recent years are beginning to unravel the molecular mechanism of this chaperone machine and how they treat their substrate proteins.
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