Disordered proteins in the ubiquitin-proteasome system
|Main area:||Molecular biology|
|Target group:||Molecular Biomedicine, Biochemistry, Biology|
|Educational level:||Masters, Bachelor|
Intrinsically disordered proteins (IDPs), that is, proteins lacking a defined 3D structure and with specific sequence characteristics, are widespread in eukaryotic cells, where they often function in cell signaling. Recent studies have shown that a number of IDPs play important roles in the ubiquitin-proteasome system, e.g. as proteasome subunits or E3 ubiquitin-protein ligases. Using human tissue culture cells and/or the fission yeast Schizosaccharomyces pombe as model organisms, projects aimed at functional characterization of selected IDPs are available. The projects will include a variety of genetic, biochemical and molecular biological techniques including co-immunoprecipitation, Western blotting, yeast two-hybrid analyses, genetic screens, and various cell biological techniques, such as pulse-chase experiments and fluorescence microscopy. Structural studies and mass spectrometry are performed in collaboration with other laboratories. The projects are available at the Bachelors, Masters or Ph.D. level. For further details, please contact Rasmus Hartmann-Petersen for an informal meeting.
|Methods used:||Protein chemistry, Cell biology, Molecular Biology, Genetics|
|Keywords:||ubiquitin, proteasome, disorder, structure, protein function|
|Project home page:||http://www1.bio.ku.dk/english/research/bms/research/pbg/groups/rhp/|