The Small Ones Matter-sHsps in the Bacterial Chaperone Network

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 alpha-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.

Automated summary

Small heat shock proteins (sHsps) are a class of ATP-independent chaperones that play a crucial role during protein stress, forming assemblies with aggregation-prone protein substrates to prevent irreversible aggregation. These assemblies facilitate subsequent chaperone-dependent disaggregation and refolding of substrates.