| Texto completo | |
| Autor(es): |
Batista, Fernanda A. H.
[1]
;
Seraphim, Thiago V.
[1]
;
Santos, Clelton A.
[2]
;
Gonzaga, Marisvanda R.
[1]
;
Barbosa, Leandro R. S.
[3]
;
Ramos, Carlos H. I.
[2, 4]
;
Borges, Julio C.
[1]
Número total de Autores: 7
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Inst Quim Sao Carlos, Av Trabalhador Saocarlense, 400 CP 780, BR-13560970 Sao Carlos, SP - Brazil
[2] Univ Estadual Campinas UNICAMP, Inst Quim, Rua Jose de Castro S-N, Cidade Univ, CP 6154, BR-13083970 Campinas, SP - Brazil
[3] Univ Sao Paulo, Inst Fis, Av Prof Lineu Prestes, 748, CP 26077, Sao Paulo, SP - Brazil
[4] Inst Nacl Ciencia & Tecnol Biol Estrutural & Bioi, Av Brigadeiro Trompowsky S-N, Cidade Univ, Rio De Janeiro, RJ - Brazil
Número total de Afiliações: 4
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Archives of Biochemistry and Biophysics; v. 600, p. 12-22, JUN 15 2016. |
| Citações Web of Science: | 3 |
| Resumo | |
Parasites belonging to the genus Leishmania are subjected to extensive environmental changes during their life cycle; molecular chaperones/co-chaperones act as protagonists in this scenario to maintain cellular homeostasis. Hop/Sti1 is a co-chaperone that connects the Hsp90 and Hsp70 systems, modulating their ATPase activities and affecting the fate of client proteins because it facilitates their transfer from the Hsp70 to the Hsp90 chaperone. Hop/Sti1 is one of the most prevalent co-chaperones, highlighting its importance despite the relatively low sequence identity among orthologue proteins. This multi-domain protein comprises three tetratricopeptides domains (TPR1, TPR2A and TPR2B) and two Asp/Pro-rich domains. Given the importance of Hop/Sti1 for the chaperone system and for Leishmania protozoa viability, the Leishmania braziliensis Hop (LbHop) and a truncated mutant (LbHop(TPR2AB)) were characterized. Structurally, both proteins are alpha-helix-rich and highly elongated monomeric proteins. Functionally, they inhibited the ATPase activity of Leishmania braziliensis Hsp90 (LbHsp90) to a similar extent, and the thermodynamic parameters of their interactions with LbHsp90 were similar, indicating that TPR2A-TPR2B forms the functional center for the LbHop interaction with LbHsp90. These results highlight the structural and functional similarity of Hop/Sti1 proteins, despite their low sequence conservation compared to the Hsp70 and Hsp90 systems, which are phylogenetic highly conserved. (C) 2016 Elsevier Inc. All rights reserved. (AU) | |
| Processo FAPESP: | 11/23110-0 - Uso da calorimetria de titulação isotérmica para a determinação de propriedades termodinâmicas de interação de proteína-ligante e proteína-proteína |
| Beneficiário: | Julio Cesar Borges |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| 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: | 14/07206-6 - Estudos da HSP70 mitocondrial de humanos e de protozoários: abordagem estrutural e funcional |
| Beneficiário: | Julio Cesar Borges |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |