Project Details
Projekt
Mechanism of chaperonin-mediated protein folding and assembly (A12)
Subject Area
Biochemistry
Term
from 2016 to 2024
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 201302640
A substantial fraction of newly-synthesised proteins require assistance from molecular chaperones to reach their folded states efficiently and at a biologically relevant time scale. In the second funding period, we used a combination of spectroscopic methods and cryo-electron microscopy to analyse the mechanism of the eukaryotic chaperonin TRiC/CCT in promoting protein folding and characterised the protein Hgh1 as a new chaperone that cooperates with TRiC. We now plan to investigate the function of the major chaperone Hsp70 in protein folding. We will use biophysical techniques such as spFRET and H/DX-MS to investigate whether Hsp70, like the chaperonins, can accelerate folding and, if so, by which mechanism.
DFG Programme
Collaborative Research Centres
Applicant Institution
Technische Universität München (TUM)
Project Heads
Professor Dr. Franz-Ulrich Hartl; Dr. Manajit Hayer-Hartl
