Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.

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Version: author
Serval ID
serval:BIB_C75F84952FAB
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Title
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
Journal
Cellular and Molecular Life Sciences
Author(s)
Mattoo R.U., Goloubinoff P.
ISSN
1420-9071 (Electronic)
ISSN-L
1420-682X
Publication state
Published
Issued date
2014
Peer-reviewed
Oui
Volume
71
Number
17
Pages
3311-3325
Language
english
Notes
Publication types: Journal Article Publication Status: ppublish Document Type: Review, pdf : Review
Abstract
By virtue of their general ability to bind (hold) translocating or unfolding polypeptides otherwise doomed to aggregate, molecular chaperones are commonly dubbed "holdases". Yet, chaperones also carry physiological functions that do not necessitate prevention of aggregation, such as altering the native states of proteins, as in the disassembly of SNARE complexes and clathrin coats. To carry such physiological functions, major members of the Hsp70, Hsp110, Hsp100, and Hsp60/CCT chaperone families act as catalytic unfolding enzymes or unfoldases that drive iterative cycles of protein binding, unfolding/pulling, and release. One unfoldase chaperone may thus successively convert many misfolded or alternatively folded polypeptide substrates into transiently unfolded intermediates, which, once released, can spontaneously refold into low-affinity native products. Whereas during stress, a large excess of non-catalytic chaperones in holding mode may optimally prevent protein aggregation, after the stress, catalytic disaggregases and unfoldases may act as nanomachines that use the energy of ATP hydrolysis to repair proteins with compromised conformations. Thus, holding and catalytic unfolding chaperones can act as primary cellular defenses against the formation of early misfolded and aggregated proteotoxic conformers in order to avert or retard the onset of degenerative protein conformational diseases.
Pubmed
Web of science
Open Access
Yes
Create date
19/09/2014 17:49
Last modification date
20/08/2019 16:42
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