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Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

Content Provider	Scilit
Author	Mayer, Matthias P. Gierasch, Lila M.
Copyright Year	2019
Description	Journal: Journal of Biological Chemistry Hsp70 chaperones are central hubs of the protein quality control network and collaborate with co-chaperones having a J-domain (an ∼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.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6369304/pdf http://www.jbc.org/content/294/6/2085.full.pdf
Ending Page	2097
Page Count	13
Starting Page	2085
ISSN	00219258
e-ISSN	1083351X
DOI	10.1074/jbc.rev118.002810
Journal	Journal of Biological Chemistry
Issue Number	6
Volume Number	294
Language	English
Publisher	Elsevier BV
Publisher Date	2019-02-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Chemistry 70-kilodalton Heat Shock Protein (hsp70) Allosteric Regulation Chaperone Dnaj (dnaj) Chaperone Dnak (dnak) Molecular Chaperone Protein Homeostasis
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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