Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Hartl, F. Ulrich
Location Max Planck Institute of Biochemistry
Primary Field Biochemistry
 Election Citation
Hartl is a pioneer of the protein folding field. Hartl was the first to show that chaperones assist the folding of polypeptide chains in vivo, reconstituted the pathway of chaperone-assisted folding in vitro, and discovered that protein folding takes place in the cavity of the GroEL chaperonin, a key insight.
 Research Interests
Research in my laboratory is centered on the role of molecular chaperones in protein folding in health and disease. Using mitochondria as a model system, we were able to show in the late 1980s that molecular chaperones like Hsp60 mediate the basic process of polypeptide chain folding in an ATP-dependent reaction (collaborative work with A. Horwich and W. Neupert). We then investigated the mechanism of the bacterial Hsp60, GroEL, and found that it functions together with GroES as a cage-like compartment, allowing the folding of single protein molecules to proceed unimpaired by aggregation. We also reconstituted the conserved cytosolic folding pathway in which the Hsp70 and Hsp60 chaperone systems cooperate sequentially. In other research we demonstrated the significance of co-translational domain folding as a process of particular importance in the biogenesis of large multi-domain proteins in eukaryotes. In recent years we have investigated the role of molecular chaperones in the defense against toxic protein aggregation in neurodegenerative diseases. Most recently, in collaboration with M. Hayer-Hartl, we have investigated the folding and assembly of ribulose bisphosphate carboxylase-oxygenase (Rubisco), the enzyme in plants that catalyzes the production of biomass from atmospheric carbon dioxide. This work has led to the discovery of a specific assembly chaperone for Rubisco that acts downstream of GroEL.

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