Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system

Mokry, David Z.; Silva, Viviane C. H. da; Abrahão, Josielle; Ramos, Carlos H.I.

doi:10.1007/s13562-017-0409-7

J. Plant Biochem. Biotechnol.

2017

DOI: 10.1007/s13562-017-0409-7

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Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system

David Z. Mokry

Viviane C. H. da Silva

Josielle Abrahão

et al.

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Cited by 2 publications

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“…The results with HSP70-based machinery are impressive because until recently only chaperones from the HSP100 family (for instance, CLPB in Escherichia coli and HSP104 in yeast) were known to act as disaggregases, and no representatives of this protein was found in metazoan. [8,23,32] Plants are among the organisms that present the canonical disaggregase HSP100 [33,34] and it is scientifically important to explore their HSP70-based machinery. Therefore, we asked whether a HSP110 from sorghum has the same functions as that of a mammalian HSP110, both alone and as part of a previously identified HSP70-based machinery.…”

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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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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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AtHsp101 research sets course of action for the genetic improvement of crops against heat stress

Kumar

Khungar

Shimphrui

et al. 2020

J. Plant Biochem. Biotechnol.

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Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system

Cited by 2 publications

References 51 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

AtHsp101 research sets course of action for the genetic improvement of crops against heat stress

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