The 70 KDA Heat Shock Protein Hsp70 as Part of a Protein Disaggregase System

Nogueira, Maria Luiza Caldas; Franco, Juliana Crotti; Gandelini, Gabriela de Mello; Ramos, Carlos H.I.

doi:10.1007/978-3-319-74715-6_7

Regulation of Heat Shock Protein Responses

2018

DOI: 10.1007/978-3-319-74715-6_7

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The 70 KDA Heat Shock Protein Hsp70 as Part of a Protein Disaggregase System

Maria Luiza Caldas Nogueira

Juliana Crotti Franco

Gabriela de Mello Gandelini

et al.

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2023

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“…For instance, it cooperates with HSP70 and HSP40 to form a HSP70-based machinery that stimulates protein disaggregation and reactivation. [23][24][25][26][27][28][29][30] Disaggregase machineries are ATP-dependent and have potent disaggregation and reactivation activities. In such machinery, human HSP110s (HSP105 and HSPA4/Apg-2) are essential to promote disaggregation, a result also shown for yeast Sse1/HSP70, even though this organism express a canonical HSP100 disaggregase, HSP104.…”

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Sorghum bicolorSbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays

et al. 2023

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Perturbations in the native structure, often caused by stressing cellular conditions, not only impair protein function but also lead to the formation of aggregates, which can accumulate in the cell leading to harmful effects. Some organisms, such as plants, express the molecular chaperone HSP100 (homologous to HSP104 from yeast), which has the remarkable capacity to disaggregate and reactivate proteins. Recently, studies with animal cells, which lack a canonical HSP100, have identified the involvement of a distinct system composed of HSP70/HSP40 that needs the assistance of HSP110 to efficiently perform protein breakdown. As sessile plants experience stressful conditions more severe than those experienced by animals, we asked whether a plant HSP110 could also play a role in collaborating with HSP70/HSP40 in a system that increases the efficiency of disaggregation. Thus, the gene for a putative HSP110 from the cereal Sorghum bicolor was cloned and the protein, named SbHSP110, purified. For comparison purposes, human HsHSP110 (HSPH1/HSP105) was also purified and investigated in parallel. First, a combination of spectroscopic and hydrodynamic techniques was used for the characterization of the conformation and stability of recombinant SbHSP110, which was produced folded. Second, small-angle X-ray scattering and combined predictors of protein structure indicated that SbHSP110 and HsHSP110 have similar conformations. Then, the chaperone activities, which included protection against aggregation, refolding, and reactivation, were investigated, showing that SbHSP110 and HsHSP110 have similar functional activities. Altogether, the results add to the structure/function relationship study of HSP110s and support the hypothesis that plants have multiple strategies to act upon the reactivation of protein aggregates.

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confidence: 99%

Sorghum bicolorSbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays

et al. 2023

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The 70 KDA Heat Shock Protein Hsp70 as Part of a Protein Disaggregase System

Cited by 1 publication

References 151 publications

Sorghum bicolorSbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays

Sorghum bicolorSbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays

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