CRC 1093 - Principal Investigator Michael Ehrmann
Prof. Dr. Michael Ehrmann
Phone: +49 201 183 2949
Email
Centre for Medical Biotechnology (ZMB)
Faculty of Biology
University of Duisburg-Essen
Area B: Biological Targets B1: Supramolecular ligands modulate assembly and function of HtrA proteases
B1 will assess the specific effects of supramolecular ligands on the folding, assembly, allosteric and cooperative regulation, lipid binding and functions of oligomeric HtrA proteases. In ad-dition, the encapsulation of human HTRA proteases within large CaP nanoparticles will be used for delivery of the proteases into mammalian cells. Moreover, DNA nanotubes will be generated for functional HtrA protease encapsulation in different oligomeric states via supramolecular links, and the influence of the altered microenvironment on protein function will be studied.
Read moreCurriculum Vitae
Professional career
| 2004-today | Full Professor (W3) of Microbiology, University of Duisburg-Essen |
| 1999-2007 | Established Chair, School of Biosciences, Cardiff University, UK |
| 1991-1999 | Group leader at the Department of Biology, University of Konstanz, Mentor: Prof. Dr. W. Boos |
| 1988-1991 | Postdoctoral Research Assistant with Prof. Dr. J. Beckwith, Department of Microbiology & Molecular Genetics, Harvard Medical School |
Scientific education and degrees
| 1996 | Habilitation and Venia legendi (Microbiology & Molecular Genetics) at the University of Konstanz, Mentor: Prof. Dr. W. Boos |
| 1984-1983 | Ph.D. at the University of Konstanz with Prof. Dr. W. Boos |
| 1976 - 1983 | Study of Biology (Dipl.) at the University of Konstanz, Diploma thesis with Prof. Dr. W. Boos |
Selected Publications
J. Bongard, M. Lorenz, I. R. Vetter, P. Stege, A. T. Porfetye, A. L. Schmitz, F. Kaschani, A. Wolf, U. Koch, P. Nussbaumer, B. Klebl, M. Kaiser, M. Ehrmann: Identification of Noncatalytic Lysine Residues from Allosteric Circuits via Covalent Probes. ACS Chem. Biol. 2018, Article ASAP, DOI: 10.1021/acschembio.8b00101 Publication Date (Web): April 16, 2018
S. Pöpsel, A. Sprengel, B. Sacca, F. Kaschani, M. Kaiser, C. Gatsogiannis, S. Raunser, T. Clausen, and M. Ehrmann: Determinants of amyloid fibril degradation by the PDZ protease HTRA1. Nat. Chem. Biol. 2015, 11, 862-869
N. J. Thompson, M. Merdanovic, M. Ehrmann, E. van Duijn, A. J. R. Heck: Substrate Occupancy at the Onset of Oligomeric Transitions of DegP. Structure. 2014, 22, 281–290
M. Mastny, A. Heuck, R. Kurzbauer, A. Heiduk, P. Boisguerin, R. Volkmer, M. Ehrmann, C. D. A. Rodriguez, D. Z. Rudner, T. Clausen: CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis. Cell. 2013, 155, 647–658
M. Malet, F. Canellas, J. Sawa, J. Yan, K. Thalassinos, M. Ehrmann, T. Clausen, H. Saibil: Binding of substrate proteins inside the molecular cage of the chaperone-protease DegQ. Nat. Struct. Mol.Biol. 2012, 19, 152-157
T. Clausen, M. Kaiser, R. Huber and M. Ehrmann: HtrA proteases: Regulated proteolysis in protein quality control. Nat. Rev. Mol. Cell Biol. 2011, 12, 152-162.
L. Trübestein, A. Tennstaedt, T. Mönig, T. Krojer, F. Canellas, M. Kaiser, T. Clausen, M. Ehrmann. Substrate induced remodeling of the active site regulates human HTRA1 activity. Nat. Struct. Mol. Biol. 2011, 18, 386-388.
M. Merdanovic, N. Mamant, M. Meltzer, S. Poepsel, A. Auckenthaler, R. Melgaard, P. Hauske, L. Nagel-Steger, A. R. Clarke, M. Kaiser, R. Huber, M. Ehrmann: Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nat. Struct. Mol. Biol. 2010, 17, 837-843.
T. Krojer, J. Sawa, E. Schäfer, H. R. Saibil, M. Ehrmann, T. Clausen: Structural basis for the regulated protease and chaperone function of DegP. Nature. 2008, 453, 885-890.
C. Wilken, K. Kitzing, R. Kurzbauer, M. Ehrmann, T. Clausen: Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease domain. Cell. 2004, 117, 483-494
C. Spiess, A. Beil, M. Ehrmann: A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell. 1999, 97, 339-347.
