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

Author(s)

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.

Affiliation

^[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

• Document type: Journal article
• Source: International Journal of Biological Macromolecules; v. 156, p. 522-530, AUG 1 2020.
• Web of Science Citations: 0

Abstract

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)

• FAPESP's process: 17/26131-5 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis
• Grantee: Carlos Henrique Inacio Ramos
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 16/05019-0 - The thermodynamical and structural influence of ionic liquids in biomimetic membrane models
• Grantee: Natália Fernandes de Oliveira
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• FAPESP's process: 15/15822-1 - Physicochemical and structural properties of Ionic Liquids and drugs interacting with biologicaly relevant systems.
• Grantee: Leandro Ramos Souza Barbosa
• Support Opportunities: Regular Research Grants
• FAPESP's process: 14/25967-4 - Characterization of the role of ATPase domains and human co-chaperones Hsp40 and hop in cellular mechanisms of thermal tolerance and suppression of protein aggregation
• Grantee: Natália Galdi Quel
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 12/01953-9 - Proteins under fibrillation process: a structural and spectroscopic study of the influence of denaturating agents
• Grantee: Leandro Ramos Souza Barbosa
• Support Opportunities: Regular Research Grants