Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays

Autor(es)

Franco, Juliana C. ; Nogueira, Maria L. C. ; Gandelini, Gabriela M. ; Pinheiro, Glaucia M. S. ; Goncalves, Conrado C. ; Barbosa, Leandro R. S. ; Young, Jason C. ; Ramos, Carlos H. I.

• Tipo de documento: Artigo Científico
• Fonte: Biopolymers; v. 114, n. 2, p. 12-pg., 2023-02-01.

Resumo

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. (AU)

• Processo FAPESP: 16/02137-1 - Clonagem, expressão, purificação e caracterização da proteína Hsp110 de sorgo visando a compreensão do sistema de desagregação de proteínas em plantas
• Beneficiário: Juliana Crotti Franco
• Modalidade de apoio: Bolsas no Brasil - Mestrado
• Processo FAPESP: 12/50161-8 - Estudo da estrutura e função da chaperona Hsp90 com ênfase no seu papel em homeostase celular
• Beneficiário: Carlos Henrique Inacio Ramos
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 16/14503-2 - Caracterização termodinâmica da interação da Hsp90 com outras proteínas
• Beneficiário: Maria Luiza Caldas Nogueira
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 16/04246-2 - Clonagem, expressão, purificação, caracterização biofísica e funcional de membros da família da co-chaperona Hsp110 humana com ênfase em seu papel em sistemas de desagregação de proteínas
• Beneficiário: Gabriela de Mello Gandelini
• Modalidade de apoio: Bolsas no Brasil - Mestrado
• Processo FAPESP: 16/03764-0 - Caracterização do papel do sistema HSP70 e da chaperona HSP22 como um complexo de desagregase em humanos
• Beneficiário: Conrado de Campos Gonçalves
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Doutorado
• Processo FAPESP: 18/11948-9 - Estudo do mecanismo de interação das co-chaperonas "J-domain proteins" com seus substratos e com a chaperona Hsp70
• Beneficiário: Glaucia Melina Squizato Pinheiro de Castro
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 17/26131-5 - Chaperoma: estudo da relação entre a estrutura dos seus componentes e a manutenção da proteostase
• Beneficiário: Carlos Henrique Inacio Ramos
• Modalidade de apoio: Auxílio à Pesquisa - Temático