Small heat shock proteins (sHSPs) are chaperones with well-characterized roles in heat stress, but potential roles for sHSPs in desiccation tolerance have not been as thoroughly explored. We identified nine sHSPs from the tardigrade Hypsibius exemplaris, each containing a conserved alpha-crystallin domain flanked by disordered regions. Many of these sHSPs are highly expressed. Multiple tardigrade and human sHSPs could improve desiccation tolerance of E. coli, suggesting that the capacity to contribute to desicco-protection is a conserved property of some sHSPs. Purification and subsequent analysis of two tardigrade sHSPs, HSP21 and HSP24.6, revealed that these proteins can oligomerize in vitro. These proteins limited heat-induced aggregation of the model enzyme citrate synthase. Heterologous expression of HSP24.6 improved bacterial heat shock survival, and the protein significantly reduced heat-induced aggregation of soluble bacterial protein. Thus, HSP24.6 likely chaperones against protein aggregation to promote heat tolerance. Furthermore, HSP21 and HSP24.6 limited desiccation-induced aggregation and loss of function of citrate synthase. This suggests a mechanism by which tardigrade sHSPs promote desiccation tolerance, by limiting desiccation-induced protein aggregation, thereby maintaining proteostasis and supporting survival. These results suggest that sHSPs provide a mechanism of general stress resistance that can also be deployed to support survival during anhydrobiosis.Small heat shock proteins from the tardigrade Hypsibius exemplaris are shown to provide a mechanism of stress resistance that can support not just heat tolerance but desiccation tolerance as well.

Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation / Hibshman, Jonathan D; Carra, Serena; Goldstein, Bob. - In: COMMUNICATIONS BIOLOGY. - ISSN 2399-3642. - 6:1(2023), pp. 1-10. [10.1038/s42003-023-04512-y]

Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation

Carra, Serena;
2023

Abstract

Small heat shock proteins (sHSPs) are chaperones with well-characterized roles in heat stress, but potential roles for sHSPs in desiccation tolerance have not been as thoroughly explored. We identified nine sHSPs from the tardigrade Hypsibius exemplaris, each containing a conserved alpha-crystallin domain flanked by disordered regions. Many of these sHSPs are highly expressed. Multiple tardigrade and human sHSPs could improve desiccation tolerance of E. coli, suggesting that the capacity to contribute to desicco-protection is a conserved property of some sHSPs. Purification and subsequent analysis of two tardigrade sHSPs, HSP21 and HSP24.6, revealed that these proteins can oligomerize in vitro. These proteins limited heat-induced aggregation of the model enzyme citrate synthase. Heterologous expression of HSP24.6 improved bacterial heat shock survival, and the protein significantly reduced heat-induced aggregation of soluble bacterial protein. Thus, HSP24.6 likely chaperones against protein aggregation to promote heat tolerance. Furthermore, HSP21 and HSP24.6 limited desiccation-induced aggregation and loss of function of citrate synthase. This suggests a mechanism by which tardigrade sHSPs promote desiccation tolerance, by limiting desiccation-induced protein aggregation, thereby maintaining proteostasis and supporting survival. These results suggest that sHSPs provide a mechanism of general stress resistance that can also be deployed to support survival during anhydrobiosis.Small heat shock proteins from the tardigrade Hypsibius exemplaris are shown to provide a mechanism of stress resistance that can support not just heat tolerance but desiccation tolerance as well.
2023
6
1
1
10
Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation / Hibshman, Jonathan D; Carra, Serena; Goldstein, Bob. - In: COMMUNICATIONS BIOLOGY. - ISSN 2399-3642. - 6:1(2023), pp. 1-10. [10.1038/s42003-023-04512-y]
Hibshman, Jonathan D; Carra, Serena; Goldstein, Bob
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/1299386
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