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Perception of stress and the mechanisms of molecular chaperones

Molecular chaperones are proteins that assist the (un)folding of other proteins in the cell. Chaperones assist the initial proper folding of newly synthesized proteins and serve as active components in the translocation of proteins between cellular compartments, as well as in the signal transduction. Many molecular chaperones are stress-induced proteins (HSPs). During and following stress, such as heat-shock, they are involved in the prevention of protein misfolding and aggregation in the cell. Some chaperones can also actively unfold and solubilize protein aggregates and assist in their proper refolding or in their degradation by proteases. Hence, the chaperone network provides central mechanisms for the protection and the recovery from stress-induced damaged proteins, in simple prokaryotes, as well as in complex eukaryotes. We are also interested in the mechanism for perception of heat-stress by organisms as diverse as bacteria and higher plants.

Our long-term goal is to understand the chaperone network in bacteria, plant and human, in order to better prevent protein misfolding and promote the active curing of toxic protein aggregates in bacteria, plants, and especially in the case of protein misfolding diseases in mammals. As model organisms we use enterobacteria, cyanobacteria, the moss Physcomitrella patens and the higher plant Arabidopsis thaliana. Our experimental approaches combine genetics, biochemistry and biophysics.