PhD position, Madl group Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Medical University of Graz, Austria

PhD position in the Madl group at Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Medical University of Graz, Austria
Linking arginine methylation, RG/RGG protein homeostasis, and disease

Projects starting March 1st, 2020
Application deadline: September 15th, 2019

We are looking for a motivated student in chemistry or biochemistry, to work on the mechanisms of regulation of nuclear import and phase separation in the current call of the PhD program “Molecular Medicine” in the Madl lab at the Medical University of Graz, Austria. The successful candidate will investigate key regulatory mechanisms in nuclear import and phase separation using state-of-the-art solution-state NMR, and biochemical as well as a wide range of biophysical methods (ITC, FP, SAXS). The successful candidates will thus acquire a broad biophysical expertise to resolve fascinating biological problems.

Graz: Capital of Styria in the sunny south of Austria. Graz enjoys a rich history, yet is at the same time bursting with modern life. Graz is an international scientific center, with six universities and more than 50,000 students. At the same time, Graz is an attractive (and affordable) living space and workplace. Graz is close to the Austrian alps, Italy, Hungary, and Slovenia, has its own international airport and a direct train connection to Vienna international airport.

Facilities: The Medical University of Graz is situated on the Medical Science City Graz Campus next to the University Hospital and close to the city center (5 minutes bike ride to the city center and other Graz Universities). Medical University of Graz is the hub of innovative and high-end medicine in the south of Austria, host top research groups in biological and clinical sciences, and its own state-of-the-art equipment. Access to complementary collaborations and techniques is provided through the BioTechMed-Graz network.
We offer state-of-the-art facilities for NMR spectroscopy with various high-field NMR spectrometers (including 500, 600, 700 MHz), crystallography (in-house XRD with MetalJet from end 2019), small angle X-ray scattering (in-house SAXS with MetalJet from end 2019 and sealed-tube), access to synchrotron beamtime as well as a new biochemical and biophysical lab. Access to complementary biophysical techniques is facilitated through the Integrative Structural Biology and Biophysics – Graz Initiative (ISBI) (https://biotechmedgraz.at/en/research/integrative-structural-biology-and-biophysics/).

Further information about the open project, the program, and the online application procedure are available at: http://www.medunigraz.at/DK_MCD/Call.htm and https://mug.glowbase.com/

Contact:
Tobias Madl, Ph.D.
Assoc. Prof. for Integrated Structural Biology & Metabolism Research
Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging
Molecular Biology and Biochemistry
Medical University of Graz
Neue Stiftingtalstraße 6/VI
8010 Graz
Austria

Tel.: +43 316 385 71972
eMail.: tobias.madl@medunigraz.at
Homepage: http://mbbc.medunigraz.at/

Relevant recent publications:
Hartlmüller C., Spreitzer E., Göbl C., Falsone F., Madl T., NMR Characterization of Solvent Accessibility and Transient Structure in Intrinsically Disordered Proteins, Journal of Biomolecular NMR (2019) in press
Merle A.A., Witternigg A., Tam-Amersdorfer C., Hartlmüller C., Spreitzer E., Schrank E., Wagner-Lichtenegger S., Zangger K., Kungl A.J., Madl T.*, Meyer N.H.*, Falsone F.S.*, Increased aggregation tendency of alpha-Synuclein in a fully disordered protein complex, Journal of Molecular Biology (2019) in press
Hartlmüller C., Günther J.C., Wolter A.C., Wöhnert J., Sattler M., Madl T., RNA structure refinement using NMR solvent accessibility data, Scientific Reports 7 (2017) 5393
Göbl C., Resch M., Strickland M., Hartlmüller C., Viertler M., Tjandra N., Madl T., Increasing the chemical shift dispersion of unstructured proteins with a covalent lanthanide shift reagent, Angewandte Chemie 55 (2016) 14847-14851
Hartlmüller C., Göbl C., Madl T., Protein structure prediction using surface accessibility data, Angewandte Chemie 55 (2016) 11970-11974
Hofweber M., Hutten S., Bourgeois B., Spreitzer E., Niedner-Boblenz A., Schifferer M., Ruepp M.D., Simons M., Niessing D., Madl T., Dormann D., Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation, Cell 173 (2018) 706-719
Anvarian Z., Nojima H., van Kappel E.C., Madl T., Spit M., Viertler M., Jordens I., Low T.Y., van Scherpenzeel R., Kuper I., Richter K., Heck A.J.R., Boelens R., Vincent J.P., Rüdiger S.G.D., Maurice M.M., Cancer mutations derail Wnt signaling via conformational conversion of the scaffold protein Axin, Nature Structural and Molecular Biology 23 (2016) 324-332
Lorenz O., Freiburger F., Rutz D., Krause M., Zierer B., Alvira A., Cuéllar J., Valpuesta J.M., Madl T.*, Sattler M.*, Buchner J.*, Modulation of the Hsp90 chaperone cycle by a stringent client protein, Molecular Cell 53 (2014) 941-953
Karagöz G.E., Duarte A.M.S., Akoury E., Ippel H., Biernat J., Luengo T.M., Radli M., Didenko T., Nordhues B.A., Veprintsev D.P., Dickey C., Mandelkow E., Zweckstetter M., Boelens R., Madl T.*, Rüdiger S.G.D.*, Hsp90-Tau complex reveals molecular basis for specificity in chaperone action, Cell 156 (2014) 963-974
 

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Tobias Madl, Ph.D.
Assoc. Prof. for Integrated Structural Biology & Metabolism Research
Visiting Professor/FJIRSM, Chinese Academy of Sciences, Xiamen, China

 
Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging
Molecular Biology and Biochemistry
Medical University of Graz
Neue Stiftingtalstraße 6/VI
8010 Graz
Austria

 
Tel.: +43 316 385 71972
Fax.: +43 316 385 79615
eMail.: tobias.madl@medunigraz.at
Homepage: http://mbbc.medunigraz.at/