Structural characterization of chaperone modulated protein aggregation in S. cervisiae (B02)

• Subject Area: Biophysics
• Term: from 2007 to 2010
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 25065445

Prions are proteinaceous elements which are able to switch their conformation from a soluble form into an aggregated state. In yeast, the molecular chaperone Hsp104 is essential to develop the prion phenotype. It could be demonstrated that the prion phenotype in yeast has an effect on both phenotypic plasticity and the exposure of hidden genetic variations. Prions and chaperones represent dynamic modules which participate in regulation of cellular processes. The goal of the project is to obtain a better understanding of the interactions between yeast prion proteins Sup35/Ure2p and the chaperone complex consisting of Hsp104, Hsp70 and Hsp40 at atomic resolution. In order to achieve this goal, we are employing a combination of solution and solidstate NMR methods.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 740: From Molecules to Modules: Organisation and Dynamics of Functional Units in Cells
• Applicant Institution: shared FU Berlin and HU Berlin through:; Charité - Universitätsmedizin Berlin
• Co-Applicant Institution: Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP); im Forschungsverbund Berlin e.V.
• Project Head: Professor Dr. Bernd Reif