| Full text | |
| Author(s): |
Franco, Juliana C.
;
Nogueira, Maria L. C.
;
Gandelini, Gabriela M.
;
Pinheiro, Glaucia M. S.
;
Goncalves, Conrado C.
;
Barbosa, Leandro R. S.
;
Young, Jason C.
;
Ramos, Carlos H. I.
Total Authors: 8
|
| Document type: | Journal article |
| Source: | Biopolymers; v. 114, n. 2, p. 12-pg., 2023-02-01. |
| Abstract | |
Perturbations in the native structure, often caused by stressing cellular conditions, not only impair protein function but also lead to the formation of aggregates, which can accumulate in the cell leading to harmful effects. Some organisms, such as plants, express the molecular chaperone HSP100 (homologous to HSP104 from yeast), which has the remarkable capacity to disaggregate and reactivate proteins. Recently, studies with animal cells, which lack a canonical HSP100, have identified the involvement of a distinct system composed of HSP70/HSP40 that needs the assistance of HSP110 to efficiently perform protein breakdown. As sessile plants experience stressful conditions more severe than those experienced by animals, we asked whether a plant HSP110 could also play a role in collaborating with HSP70/HSP40 in a system that increases the efficiency of disaggregation. Thus, the gene for a putative HSP110 from the cereal Sorghum bicolor was cloned and the protein, named SbHSP110, purified. For comparison purposes, human HsHSP110 (HSPH1/HSP105) was also purified and investigated in parallel. First, a combination of spectroscopic and hydrodynamic techniques was used for the characterization of the conformation and stability of recombinant SbHSP110, which was produced folded. Second, small-angle X-ray scattering and combined predictors of protein structure indicated that SbHSP110 and HsHSP110 have similar conformations. Then, the chaperone activities, which included protection against aggregation, refolding, and reactivation, were investigated, showing that SbHSP110 and HsHSP110 have similar functional activities. Altogether, the results add to the structure/function relationship study of HSP110s and support the hypothesis that plants have multiple strategies to act upon the reactivation of protein aggregates. (AU) | |
| FAPESP's process: | 16/02137-1 - Cloning, expression, purification and characterization of sorghum Hsp110 protein aimed at understanding of protein disaggregation system in plants |
| Grantee: | Juliana Crotti Franco |
| Support Opportunities: | Scholarships in Brazil - Master |
| 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 Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 16/14503-2 - Thermodynamic characterization of Hsp90 interaction with other proteins |
| Grantee: | Maria Luiza Caldas Nogueira |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 16/04246-2 - Cloning, expression, purification, biophysical and functional characterization of members of the human Hsp110 family co-chaperone with emphasis on its role in protein disaggregation systems |
| Grantee: | Gabriela de Mello Gandelini |
| Support Opportunities: | Scholarships in Brazil - Master |
| FAPESP's process: | 16/03764-0 - Characterization of the role of HSP70 system and HSP22 chaperone as a disaggregase complex in humans |
| Grantee: | Conrado de Campos Gonçalves |
| Support Opportunities: | Scholarships abroad - Research Internship - Doctorate |
| FAPESP's process: | 18/11948-9 - Interaction mechanism between the co-chaperone J-domain protein with their substrates and the chaperone Hsp70 |
| Grantee: | Glaucia Melina Squizato Pinheiro de Castro |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| 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 |