Heat shock protein 90 kDa (Hsp90) from Aedes aegypti has an open conformation and is expressed under heat stress

Autor(es)

Quel, Natalia G. ^[1] ; Pinheiro, Glaucia M. S. ^[1] ; Rodrigues, Luiz Fernando de C. ^[2] ; Barbosa, Leandro R. S. ^[2] ; Houry, Walid A. ^{[3, 4]} ; Ramos, I, Carlos H.

Afiliação do(s) autor(es)

^[1] I, Univ Estadual Campinas, Inst Chem, UNICAMP, BR-13083970 Campinas, SP - Brazil

^[2] Univ Sao Paulo, Inst Phys, BR-05508090 Sao Paulo, SP - Brazil

^[3] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8 - Canada

^[4] Univ Toronto, Dept Chem, Toronto, ON M5S 3H6 - Canada

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 156, p. 522-530, AUG 1 2020.
• Citações Web of Science: 0

Resumo

Cellular proleostasis is maintained by a system consisting of molecular chaperones, heat shock proteins (Hsps) and proteins involved with degradation. Among the proteins that play important roles in the function of this system is Hsp90, which acts as a node of this network, interacting with at least 10% of the proteome. Hsp90 is ATP-dependent, participates in critical cell events and protein maturation and interacts with large numbers of cochaperones. The study of Hsp90 orthologs is justified by their differences in ATPase activity levels and conformational changes caused by Hsp90 interaction with nucleotides. This study reports the characterization of Hsp90 from Aedes aegypti, a vector of several diseases in many regions of the planet. Aedes aegypti Hsp90, AaHsp90, was cloned, purified and characterized for its ATPase and chaperone activities and structural conformation. These parameters indicate that it has the characteristics of eukalyotic Hsp90s and resembles orthologs from yeast rather than from human. Finally, constitutive and increased stress expression in Aedes cells was confirmed. Taken together, the results presented here help to understand the relationship between structure and function in the Hsp90 family and have strong potential to form the basis for studies on the network of chaperone and Hsps in Aedes. (C) 2020 Elsevier B.V. All rights reserved. (AU)

• 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
• Processo FAPESP: 16/05019-0 - A influência termodinâmica e estrutural de líquidos iônicos em sistemas biomiméticos de membrana
• Beneficiário: Natália Fernandes de Oliveira
• Modalidade de apoio: Bolsas no Brasil - Iniciação Científica
• Processo FAPESP: 15/15822-1 - Estudo das propriedades físico-químicas e estruturais de fármacos e líquidos iônicos com sistemas de relevância biológica
• Beneficiário: Leandro Ramos Souza Barbosa
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 14/25967-4 - Caracterização do papel de domínios ATPase e das co-chaperonas Hsp40 e hop humanas nos mecanismos celulares de termotolerância e supressão de agregação proteica
• Beneficiário: Natália Galdi Quel
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 12/01953-9 - Proteínas em condição de fibrilação: caracterização estrutural e espectroscópica em função de agentes desnaturantes
• Beneficiário: Leandro Ramos Souza Barbosa
• Modalidade de apoio: Auxílio à Pesquisa - Regular