Protein-Repair Machineries: Evolution and Function

This lecture explores the evolution of protein-repair machineries across different life forms, focusing on their role in preventing protein aggregation and promoting proper folding. It discusses the relationships between chaperones and cochaperones, emphasizing the importance of ATP-fueled unfolding machines in cellular proteostasis. The lecture delves into the concept of injecting free energy into stable aggregates to facilitate the refolding process, highlighting the catalytic role of unfolding enzymes in protein folding. It also touches upon the emergence of molecular chaperones before the first eukaryote and the expansion of chaperones in more complex organisms. The speaker presents insights into the functional hierarchy of the chaperone network, with HSP70 playing a central role in cellular protein quality control.