| Full text | |
| Author(s): |
Quel, Natalia G.
[1, 2]
;
Rodrigues, Luiz Fernando de C.
[3]
;
Aragao, Annelize Z. B.
[1]
;
Pinheiro, Glaucia M. S.
[1]
;
Camacho, Rafael P.
[1]
;
Souto, Denio E. P.
[4]
;
Kubota, Lauro T.
[1, 5]
;
Barbosa, Leandro R. S.
[3, 6]
;
Ramos, Carlos H. I.
[1, 2]
Total Authors: 9
|
| Affiliation: | [1] Univ Estadual Campinas, UNICAMP, Inst Chem, BR-13083970 Campinas, SP - Brazil
[2] Natl Inst Sci Technol Struct Biol & Bioimage INCT, Sao Carlos - Brazil
[3] Univ Sao Paulo, Inst Phys, BR-05508090 Sao Paulo, SP - Brazil
[4] Fed Univ Paran UFPR, Dept Chem, BR-81530900 Curitiba, PR - Brazil
[5] Natl Inst Sci & Technol Bioanalyt INCTBio, Campinas - Brazil
[6] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Synchrotron Light Lab LNLS, Campinas - Brazil
Total Affiliations: 6
|
| Document type: | Journal article |
| Source: | Biochimie; v. 187, p. 131-143, AUG 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
SGTs (small glutamine-rich TPR-containing proteins) are dimeric proteins that belong to the class of co-chaperones characterized by the presence of TPR domains (containing tetratricopeptide repeats). Human (SGTA) and yeast (Sgt2) SGTs are characterized by three distinct domains: an N-terminal dimerization domain, a central TPR-domain important for binding to other proteins (chaperones included) and a C-terminal domain involved in hydrophobic interactions. Both these SGTs are involved in the cellular PQC (protein quality control) system, as they interact with chaperones and have functions that aid stress recovery. However, there are differences between them, such as structural features and binding specificities, that could be better understood if other orthologous proteins were studied. Therefore, we produced and characterized a putative SGT protein, designated AaSGT, from the mosquito Aedes aegypti, which is a vector of several diseases, such as dengue and Zika. The protein was produced as a folded dimer which was stable up to 40 degrees C and was capable of binding to AaHsp90 and fully protecting a model protein, alpha-synuclein, from aggregation. The conformation of AaSGT was investigated by biophysical tools and small angle X-ray scattering, which showed that the protein had an elongated conformation and that its C-terminal domain was mainly disordered. The results with a C-terminal deletion mutant supported these observations. Altogether, these results are consistent with those from other functional SGT proteins and add to the understanding of the PQC system in Aedes aegypti, an important aim that may help to develop inhibitory strategies against this vector of neglected diseases. (C) 2021 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU) | |
| 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: | 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 |
| 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: | 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: | 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 |