Journal
FRONTIERS IN MOLECULAR BIOSCIENCES
Volume 8, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fmolb.2021.666893
Keywords
protein aggregation; protein refolding; holdase activity; chaperones; small heat shock proteins (sHsps); proteotoxic stress; Hsp70– Hsp100 dependent disaggregation
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Funding
- Polish National Science Centre [OPUS 17 2019/33/B/NZ1/00352]
- START program from Foundation for Polish Science [63.2020]
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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.
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.
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