Cloning, expression, purification and characterization of sorghum Hsp110 protein aimed at understanding of protein disaggregation system in plants

• Grant number: 16/02137-1
• Support Opportunities: Scholarships in Brazil - Master
• Start date: May 01, 2016
• End date: February 28, 2018
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Carlos Henrique Inacio Ramos
• Grantee: Juliana Crotti Franco
• Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil

Abstract

The importance of proteins for the operation of the cell can be confirmed by the fact that these biomolecules participate in nearly all physiological events in an organism. For a large group of proteins be functional depends on obtaining a three dimensional structure that is stable, or native. The loss of the native structure often caused by stress cellular conditions, not only causes loss of function but may also lead to the formation of protein aggregates, which can accumulate in the cell with damaging effects for the same. Some organisms, such as plants for example, developed a system composed of the molecular chaperones Hsp70 and Hsp100, which has the amazing ability to disaggregate and refold these proteins. Recently, studies in animal cells, which have no Hsp100, identified the participation of co-chaperone Hsp110 with Hsp70 in an efficient system for the protein disaggregation. As plants face more severe stressful conditions because they are sessile, we wonder if the Hsp110 also develops a role of disaggregation in these organisms and whether it can cooperate with the Hsp100 system to increase the efficiency of the disaggregation in the plant cells. To answer these questions, we initially identified a gene for Hsp110 in sorghum and we propose clone it and test it, alone and in conjunction with other plant chaperones (Hsp70, Hsp100 and co-chaperone Hsp40, which have already been characterized by our research group) for their ability to reactivate protein aggregates. The results obtained have the potential to contribute to our knowledge of plants cellular biology and in biotechnology processes, since such systems can be used in the construction of vegetables or microorganisms that produce commercially important proteins. (AU)

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)

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.. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays. Biopolymers, v. 114, n. 2, p. 12-pg., 2023-02-01. (16/02137-1, 12/50161-8, 16/14503-2, 16/04246-2, 16/03764-0, 18/11948-9, 17/26131-5)

Academic Publications

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

FRANCO, Juliana Crotti. Cloning, expression, purification and characterization of sorghum Hsp110 protein to understanding the protein disaggregation system in plants. 2018. Master's Dissertation - Universidade Estadual de Campinas (UNICAMP). Instituto de Química Campinas, SP.