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Structural and functional studies of cytoskeleton regulation by post-translational lysine-acetylation

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Institution information: The group links the SFB635 (Post-translational control of protein function) and the CECAD (The Cologne Cluster of Excellence in Cellular Stress Responses in Aging-associated Diseases).

Location: The group is located at the CECAD Research Center, University of Cologne Joseph-Stelzmann-Str. 26, 50931 Cologne, Germany.  The Cologne research community including the University of Cologne, the University Hospital of Cologne, the CECAD and the Max-Planck-Institute for Biology of Aging is a highly stimulating and international academic research environment.

Summary: Regulation of protein function by lysine-acetylation has only been marginally functionally and mechansitically investigated so far. Recent progress in quantitative mass spectrometry has demonstrated that thousands of non-histone proteins are acetylated in mammalian cells in all cellular compartments.
The cytoskeleton has been in centre of scientific interest for many years. It contains hundreds of accessory proteins and is essential for many cellular processes: apoptosis, cell shape, transport processes, cell migration, wound healing, replication, cell differentiation and cell signaling. Deregulation and aberrations in cytoskeletal-proteins lead to several severe diseases in the human body comprising muscle- and neurodegenerative disorders, cancer and cardiovascular diseases.
The formin protein FMNL2 is an actin polymerization factor elongating unbranched actin filaments. Recently, it was shown that the small GTP-binding protein Cdc42 contacts the N-terminal domain of the formin FMNL2 via its insert helix, a unique structural feature of Rho-proteins. Cdc42 was shown to be lysine-acetylated within the insert-helix. Mutation of residues within the Rho-insert helix in Rac1 to the analogous residues in Cdc42 creates binding towards FMNL2 showing that the Rho-insert helix is crucial for the interaction. We want to understand how acetylation within the Cdc42-insert helix interferes with FMNL2 binding and function. Towards this end, we are using cell biological, biochemical and biophysical methods including X-ray crystallography.

Job description: We search for a highly motivated student with profound knowledge in proteinbiochemistry (protein-purification, -expression in E. coli). We will perform various biophysical assays (isothermal-titration calorimetry, fluorescence assays, stopped-flow, X-ray crystallography, etc.). Expression of K to Q acetylation mimetic and K to R charge conserving mutants in mammalian cells will show an effect of lysine-acetylation in vivo.
 
Qualification: Applicants must have a Bachelor of Science degree in biology /biochemistry/biophysics or related subject. Solid experience in proteinbiochemistry (including protein-purification/-expression), is advantagous but not a must. Additionally, knowledge in cell biology is advantagous. Profound experience in molecular biological methods (cloning, mutagenesis, western blotting, etc.) is essential.

How to Apply: Send a short cover letter, CV, certificates and address of one scientific reference as single PDF-document to michael.lammers@uni-koeln.de

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Art des Bewerbungszugangs
How to Apply: Send a short cover letter, CV, certificates and address of one scientific reference as single PDF-document to michael.lammers@uni-koeln.de.
 
Kontakt für Bewerbungen

michael.lammers@uni-koeln.de

Details der Stellenanzeige


Arbeitszeit
Vollzeit
Vertragslaufzeit
Befristete Anstellung
Stellentyp
Diplom- & Masterarbeit
Berufserfahrung
Berufserfahrung nicht vorausgesetzt
Region
Deutschland (Nordrhein-Westfalen)
Arbeitsort
50931 Cologne, Germany
Fachgebiet
Biologie & Life Sciences
JETZT BEWERBEN