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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome

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Silva, Noeli S. M. [1, 2] ; Seraphim, Thiago V. [1] ; Minari, Karine [1, 2] ; Barbosa, Leandro R. S. [3] ; Borges, Julio C. [1]
Total Authors: 5
[1] Univ Sao Paulo, Sao Carlos Inst Chem, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Fed Sao Carlos, Ctr Biol & Hlth Sci, BR-13560970 Sao Carlos, SP - Brazil
[3] Univ Sao Paulo, Inst Phys, Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 108, p. 193-204, MAR 2018.
Web of Science Citations: 3

The p23 proteins are small acidic proteins that aid the functional cycle of the Hsp90 molecular chaperone. Such co-chaperone acts by temporarily inhibiting the ATPase activity of Hsp90 and exhibits intrinsic chaperone activity, suggesting independent roles. A search for p23 in the Plasmodium falciparum genome led to the identification of two putative proteins showing 13% identity to each other and approximately 20% identity to human p23. To understand the presence of two p23 proteins in this organism, we generated recombinant p23 proteins (Pfp23A and Pfp23B) and investigated their structure and function. The proteins presented some similarities and dissimilarities in structural contents and showed different chemical and thermal stabilities, with Pfp23A being more stable than Pfp23B, suggesting that these proteins may present different functions in this organism. Both Pfp23 proteins behaved as elongated monomers in solution and were capable of preventing the thermal-induced aggregation of model client proteins with different efficiencies. Finally, the Pfp23 proteins inhibited the ATPase activity of recombinant P. falciparum Hsp90 (PfHsp90). These results validate the studied proteins as p23 proteins and co-chaperones of PfHsp90. (C) 2017 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 13/25646-0 - Comparative functional studies of Hsp90 from different organisms
Grantee:Karine Minari
Support type: Scholarships in Brazil - Doctorate (Direct)
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 type: Regular Research Grants
FAPESP's process: 14/07206-6 - Studies of the mitochondrial HSP70 of human and protozoa: structural and functional approaches
Grantee:Julio Cesar Borges
Support type: Regular Research Grants
FAPESP's process: 11/23110-0 - Using isothermal titration calorimetry for the determination of thermodynamic properties of protein-ligand and protein-protein interactions
Grantee:Julio Cesar Borges
Support type: Regular Research Grants
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 type: Regular Research Grants
FAPESP's process: 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis
Grantee:Carlos Henrique Inacio Ramos
Support type: Research Projects - Thematic Grants
FAPESP's process: 17/07335-9 - Studies of human HSP70 isoforms residing in the cytoplasm and mitochondria and their high molecular weight oligomers: interaction with co-chaperones and client proteins
Grantee:Julio Cesar Borges
Support type: Regular Research Grants