Study of important chaperone-interaction from the celular protein quality control system in higher eukaryotes.

• Grant number: 14/00076-0
• Support Opportunities: Scholarships in Brazil - Doctorate
• Start date: April 01, 2014
• End date: August 27, 2018
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Carlos Henrique Inacio Ramos
• Grantee: Conrado de Campos Gonçalves
• Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Associated research grant: 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis, AP.TEM
• Associated scholarship(s): 16/03764-0 - Characterization of the role of HSP70 system and HSP22 chaperone as a disaggregase complex in humans, BE.EP.DR

Abstract

Proteins are responsible by a huge number of functions in cells. This functions are directly related to the proteins fold structure. The proteins folding may not occur naturally in cells, so there is a specialized system, known Protein Quality Control (PQC). The PQC is formed by the sub-system of chaperones, which facilitates the correct folding of proteins, and the sub-system proteosome, responsible for degradation. The proteins of PQC system are more express in conditions of stress, when the wrong folding is easier. The main objective of our group is understand how the PQC system works in eukariotes, specially in human and plants. This project has the objetive of investigate the interactions among chaperones and Hsps considered relevant for the function of the PQC system. Thus, the specifics objectives are: 1) Cloning, express, purify and characterize the co-chaperone CHIP in a plant. This protein has a bind domain to Hsp70 and Hsp90 chaperones and other domain that interacts with E3 ubiquitin-ligase, so this protein is an important link between the two sub-system of the PQC. 2) Investigate the mechanisms of interaction between Hsp100 and smHsps in plants. 3) Compare the conformation of four Hsp40 human chaperones and chacterize its interactions with unfold proteins and Hsp70

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

GONCALVES, CONRADO DE C.; PINHEIRO, GLAUCIA M. S.; DAHLSTROM, KATHE M.; SOUTO, DENIO E. P.; KUBOTA, LAURO T.; BARBOSA, LEANDRO R. S.; RAMOS, I, CARLOS H.. On the structure and function of Sorghum bicolor CHIP (carboxyl terminus of Hsc70-interacting protein): A link between chaperone and proteasome systems. Plant Science, v. 296, JUL 2020. (17/26158-0, 18/11948-9, 17/26058-6, 14/00076-0, 16/14228-1, 12/50161-8, 15/15822-1)

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

GONÇALVES, Conrado de Campos. Structural and functional characterization of chaperones involved in the solubilization of protein aggregates: the role of CHIP from Sorghum bicolor and HspB1 in the human disaggregation system. 2018. Doctoral Thesis - Universidade Estadual de Campinas (UNICAMP). Instituto de Biologia Campinas, SP.