Prof. Dr. Ulrich Hartl

Project description: Research in Hartl and Hayer-Hartl laboratory focuses on the mechanisms of protein folding and quality control in the cell. Our goal is to reach a comprehensive understanding, at the structural and functional level, of how the machinery of molecular chaperones assists folding through the co­operation of co- and post-translational mechanisms. A long-standing interest is to understand how the cylindrical chaperonins of the GroEL type promote and modulate the folding process. Our second major research focus concerns the mo­lecular mechanisms of proteotoxicity in diseases associated with protein misfolding and aggregation, including Parkinson’s, Alzheimer’s, and Huntington’s diseases. Here we wish to understand how the cellular machinery of protein homeostasis (proteostasis) normally pro­vides protection and why these defense mechanisms increasingly fail during aging, facilitating the mani­festation of neurodegeneration. We are using a wide range of methods from cellular biochemistry, biophysics, and structural biology. In understanding the proteostasis network we are increasingly using systems-based approaches, including quantitative proteomics and genetic screens. An additional interest in the Hayer-Hartl group is to define the chaperone machinery involved in the folding and assembly of the photosynthetic enzyme Rubisco, as well as to understand the assembly of carboxysomes, metabolic compartments for carbon dioxide concentration and Rubisco activity.

Necessary skills in biochemistry, biophysics, and cell biology.