Anfinsen received the Nobel price in 1972 for discovering the fundamental principle that polypeptide chains may spontaneously reach their native conformation without assistance from other macromolecules. Yet, in 1989 Lorimer and collaborators found that the bacterial protein GroEL controlled the folding assembly of recombinant proteins in the crowded environment of bacterial cells (Goloubinoff et al., 1989 Nature 337, 44-47). Moreover, it was demonstrated in vitro that the chaperone GroEL can passively prevent the aggregation of artificially unfolded proteins and use the energy of ATP hydrolysis to promote the proper refolding of misfolded protein species to their native state (Goloubinoff et al., 1989 Nature 342, 884-889). Twenty-five years ago these seminal findings opened a new field of research that focused on the post-translational events in the life of proteins. Processes such as folding, translocation, misfolding, native assembly or toxic aggregation may necessitate, in the complex environment of the cell cytoplasm, the passive assistance of “holding chaperones” and the active intervention of unfolding and disaggregating chaperones.

The research on the molecular mechanisms by which various chaperones regulate protein homeostasis generated, since 1989, over 20’000 scientific publications, which contributed to the understanding of the causes for cell ageing, neurodegenerative diseases, for the resistance of cancers to chemotherapy and for the failure of various organisms, such as land plants and humans, to withstand extreme abiotic stresses, heat-shock in particular.

The purpose of this 2 days mini-symposium is to gather on this 25th anniversary, the protagonists that contributed to the initial discovery of molecular chaperones and that are still active experimentalists, and also bring from the US, Europe, Israel and Japan a number of key group leaders in the field of GroEL and CCT chaperonins (see tentative program below).

Program

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