The mitochondrial outer membrane plays a crucial role in the biogenesis, inheritance and dynamics of the organelle and forms the functional and signaling link between mitochondria and the rest of the eukaryotic cell. This membrane contains a diverse set of proteins that are synthesized in the cytosol and harbor signals that are essential for their subsequent import into mitochondria. We investigate the molecular mechanisms by which the various mitochondrial outer membrane proteins are targeted to mitochondria, inserted into the outer membrane and assembled into functional complexes within the membrane. In addition, we study the mechanisms and components that regulate lipids homeostasis in mitochondria. For our studies we use both yeast and mammalian tissue cultures as experimental systems.
- Biogenesis of mitochondrial and bacterial β-barrel proteins
- Cytosolic factors that mediate targeting of mitochondrial precursor proteins
- Membrane integration of mitochondrial outer membrane helical proteins
- Lipid homeostasis in mitochondria
- we investigate several regulators of apoptosis and alternate cell death modes,
- characterize cellular senescence as a tumor suppressor and immune-modulatory mechanism,
- explore new regulators of transcription factor NF-κB,
- study the involvement of stress pathways in the reprogramming of differentiated cells to induced pluripotent stem cells,
- elucidate the correlation between DNA damage, DNA repair, stem cell differentiation and cell death,
- conduct translational projects using novel biomarkers of cell death and senescence for monitoring anticancer treatment and tissue damage.
All eukaryotes organize their genomes in the form of chromatin, a complex of DNA and dedicated packing proteins, so-called histones. In addition to compacting DNA, chromatin regulates the activity of encoded genes through posttranslational modifications of the histone proteins. Deciphering the complex crosstalk between histone modifications and gene activity represents a central challenge for biomedical science. Our group is developing and using chemical tools to study the physiological function of posttranslational histone modifications. To this end we combine methods from chemistry, biochemistry and molecular biology to probe a wide range of chromatin factors including chromatin binding proteins and histone-modifying enzymes.
Nucleic acids are fantastic molecules. Due to their unique base pairing properties, hybridization between nucleic acids is highly predictable and thus rationally programmable. We develop artifical, RNA-guided machines with the intention to create practical tools for the study and control of basic biochemical processes like RNA processing, translation, or epitranscriptomics. To achieve our goals, we combine chemistry with biotechnology and create tools that we optimize for application inside cells and living organisms.
We try to uncover the precise atomic architecture of one of life's key molecules, the protein. For example, we look at the proteins crucial for virus infection. These molecules sit on the surface of the virus particle and enable it to enter the host cell. We also look at the make-up of bacterial proteins and try to pinpoint their weak spots which may become the target of a future drug. In addition, based on their structure, we try to deduce how receptor proteins on the cell surface do their jobs of relaying information from the outside to the inside of the cell.