Study of Hsp90 interaction with other proteins by cross-linking and investigation of metals binding and their effects

• Grant number: 14/00170-6
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• Start date: April 01, 2014
• End date: April 30, 2016
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Carlos Henrique Inacio Ramos
• Grantee: Dev Sriranganadane
• 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): 15/21930-1 - Deciphering structural information of Hsp90 chaperone complexed with hop and chip co-chaperones using high resolution mass spectrometry and chemical cross-link, BE.EP.PD

Abstract

The fact that Hsp90 can be considered a hub-protein, i.e. has a large number of interaction in the cell, demonstrate the importance to study this chaperone. Hsp90 interacts with at least 10% of the expressed proteins in eukaryotes. However, little information exists about the regions of interaction due to the high molecular mass of Hsp90 and because some interactions are only transient. It is also difficult to populate the partner proteins at the high concentration necessary for standard studies. In addition to the above there is also little information about other factors that affect the interaction of Hsp90 with proteins. We intend to use mass spectrometry, in collaboration with experts in the field, to investigate the regions of interaction between Hsp90 and other proteins by covalent crosslinking and the effect that metals have on the structure and function of Hsp90. The large-scale study of the effect of metals in proteins has recently gained relevance in chaperones and their application can not be ignored.