The ensemble of molecular chaperones constitutes the cellular system that assists folding and assembly of newly synthesized proteins, translocation of unfolded proteins across membranes, as well as refolding and degradation of misfolded and aggregated proteins. The long term goal of our research is to understand the intricate functional network of chaperones and proteases in the cytosol of bacteria. We are aiming at unraveling how ribosome-associated chaperones and folding enzymes interact with and assist the co-translational folding of nascent polypeptides. We are also interested in understanding the role of AAA-chaperones in protein quality control. AAA-chaperones form ring-shaped oligomers that use the energy of ATP to bind, unfold and translocate polypeptides through their central pore. This activity is employed by ClpB (Hsp104) for solubilization and refolding of aggregated proteins, and by ClpA for targeting substrates for degradation by an associated peptidase.
Bernd Bukau (*1954 in Leipzig) is director of the Centre of Molecular Biology in Heidelberg (ZMBH). He studied Biology in Konstanz and at the University of California, Santa Cruz. His main fields of interest are cellular stress response, molecular chaperones and proteases as well as protein folding and quality control. Professor Bukau received the Leibniz Prize of the German Research Foundation (DFG) and is an elected member of the German Academy of Sciences Leopoldina.
Moderation: Professor Dr. Michael Hecker