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Title of the item:

The Small Ones Matter—sHsps in the Bacterial Chaperone Network

Title :
The Small Ones Matter—sHsps in the Bacterial Chaperone Network
Authors :
Igor Obuchowski
Piotr Karaś
Krzysztof Liberek
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Subject Terms :
protein aggregation
protein refolding
holdase activity
small heat shock proteins (sHsps)
proteotoxic stress
Biology (General)
Source :
Frontiers in Molecular Biosciences, Vol 8 (2021)
Publisher :
Frontiers Media S.A., 2021.
Publication Year :
Collection :
LCC:Biology (General)
Document Type :
File Description :
electronic resource
Language :
Relation :;
Access URL :
Accession Number :
Academic Journal
Small heat shock proteins (sHsps) are an evolutionarily conserved class of ATP-independent chaperones that form the first line of defence during proteotoxic stress. sHsps are defined not only by their relatively low molecular weight, but also by the presence of a conserved α-crystallin domain, which is flanked by less conserved, mostly unstructured, N- and C-terminal domains. sHsps form oligomers of different sizes which deoligomerize upon stress conditions into smaller active forms. Activated sHsps bind to aggregation-prone protein substrates to form assemblies that keep substrates from irreversible aggregation. Formation of these assemblies facilitates subsequent Hsp70 and Hsp100 chaperone-dependent disaggregation and substrate refolding into native species. This mini review discusses what is known about the role and place of bacterial sHsps in the chaperone network.

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