Clausen Group
Tim Clausen (Senior Scientist)
Molecular mechanisms of protein quality control
The misfolding and aggregation of protein molecules is a major threat to all living organisms. Cells have therefore evolved a sophisticated network of molecular chaperones and proteases to prevent protein aggregation (Fig. 1A). In addition, protein quality control and regulatory proteolysis are important mechanisms in the defense line of several bacterial pathogens. My group is performing a structure-function analysis of prokaryotic and eukaryotic factors that combat folding stress and, in parallel, ensure controlled digestion of specific target proteins. A better understanding of protein quality control might disclose novel strategies to counteract protein folding diseases and bacterial pathogenicity.
Movie 1: The protease-chaperone DegP at work.
Selected Publications
- Gazda, L., Pokrzywa, W., Hellerschmied, D., Löwe, T., Forné, I., Mueller-Planitz, F., Hoppe, T., Clausen, T. (2013). The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegans. Cell. 152(1-2):183-95 (abstract)
- Fuhrmann, J., Schmidt, A., Spiess, S., Lehner, A., Turgay, K., Mechtler, K., Charpentier, E., Clausen, T. (2009). McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR. Science. 324(5932):1323-7 (abstract) (fulltext)
- Krojer, T., Sawa, J., Schäfer, E., Saibil, HR., Ehrmann, M., Clausen, T. (2008). Structural basis for the regulated protease and chaperone function of DegP. Nature. 453(7197):885-90 (abstract)
