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Welcome to the research group “Mechanisms of Molecular Machines”

Prof. Dr. Dagmar Klostermeier

Applications accepted until September 30 2021:

Postdoctoral position in Biophysical Chemistry /RNA biochemistry
“Sequence-encoded single-molecule imaging of RNA-protein complexes”
This project combines single-molecule microscopy with next-generation sequencing to obtain sequence-encoded information on the dynamics of protein-nucleic acid interactions on a high-throughput level. The focus will be on RNA-helicase complexes. The aim of this project is a molecular, yet transcriptome-wide understanding of the activation of helicases by RNA substrates.
The group is located at the Institute for Physical Chemistry at the University of Muenster and offers state-of-the-art molecular biology and biochemistry laboratories. A next-generation sequencer and a total internal reflection molecule microscope with fast camera detection system as well as confocal single-molecule microscopes with alternating laser excitation are available.
The successful applicant holds a doctoral degree in Biophysical Chemistry, Biochemistry, Biophysics, Chemistry, Biology, Physics, or related fields, and has a genuine interest in research, combined with experimental enthusiasm. Besides prior knowledge in molecular biology, protein and nucleic acid biochemistry, expertise in at least two of the following areas is required:
- preparation, execution and analysis of von next-generation sequencing experiments
- preparation, execution and analysis of single-molecule experiments
- implementation of microfluidic devices
- development of routines for project-specific data analysis (LabVIEW, MATLAB, etc.)
Experience with helicases or other RNA-binding proteins is a plus.
The official advertisement (in German) including detailed information on the position and the application is available under
https://www.uni-muenster.de/Rektorat/Stellen/ausschreibungen/st_20210608_sk6.html


Our lab investigates the role of ATP-driven conformational changes for the catalytic activity of helicases and topoisomerases using single-molecule FRET experiments. Helicases and topoisomerases are energy-coupling enzymes that convert the energy of ATP hydrolysis into structural changes in their substrates. RNA helicases mediate a multitude of RNA rearrangements in transcription, RNA splicing and editing, RNA export, mRNA translation, ribosome assembly, RNA degradation, and potentially RNA folding in general. In accordance with their variety of functions, they are associated with complex processes such as ageing, differentiation, and cancer. Topoisomerases change the topological state of DNA in an ATP-dependent reaction. DNA topology impacts key cellular events such as replication, transcription, recombination, and the storage of the genome as chromatin. Furthermore, cooperation between helicases and topoisomerases is required to maintain genome integrity.

To comprehensively understand the mechanisms of these enzymes and the regulation of their activities, we employ a wide variety of techniques, including molecular biology, protein and nucleic acid biochemical techniques, FPLC and HPLC chromatography, absorption, fluorescence and circular dichroism spectroscopy, steady-state and pre-steady-state kinetics, calorimetric methods, and time-resolved single-molecule fluorescence spectroscopy by confocal and total internal reflection microscopy.