The overall goal of our research is to understand the cellular pathways underlying protein biogenesis and maintenance of proteome homeostasis in eukaryotic cells. Folding of newly synthesized polypeptides as well as functional maintenance and refolding upon denaturing events are essential processes in all organisms. Failure in theses processes often results in protein misfolding and accumulation of insoluble protein aggregates with drastic consequences for cell viability.

We are particularly interested in understanding the contribution of the molecular chaperone network for protein maturation and maintenance of functionality. While many aspects of chaperone function are well studied in bacteria, the cytosol of eukaryotic organisms, the endoplasmic reticulum, and mitochondria, relatively little is understood within the chloroplast. This is surprising given the importance of this organelle for virtually all life on our planet. Chloroplasts harbor essential biochemical pathways such as photosynthesis or carbon fixation. During protein biogenesis chloroplast proteomes face a highly challenging task of integrating proteins encoded by the nuclear genome and proteins encoded by the small chloroplast genome. Thus, investigating biogenesis and maintenance of protein homeostasis in chloroplasts is essential for a general understanding of protein folding, and contributes to a evolutionary understanding how cells adapt their protein folding environment to the requirements of a sub-cellular proteome.