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Archiv-Übersicht     Angebot Nr. 13183

Angebotsdatum: 11. Dezember 2018
Art der Stelle: Doktorarbeit
Fachgebiet: Humanmedizin > Biochemie
Titel des Themas: Decoding the molecular mechanisms of membrane protein targeting and insertion

Institut: Institut für Biochemie und Molekularbiologie
Prof. Hans-Georg Koch
Stefan Meier Str. 17
79104 Freiburg
Tel.: 00497612035250   Fax.: 00497612035289
Homepage: http://https://www.biochemie.uni-freiburg.de/de/ag/koch
E-Mail Kontakt: mail

Beschreibung: The spatial and temporal coordination of protein trafficking is essential in all cells and in particular important for aggregation-prone membrane proteins. These proteins account for approximately one third of the genetic coding capacity in an average organism and they are crucially important for sustaining metabolic activity and intercellular communication. Reflecting their importance, cells use sophisticated strategies for routing membrane proteins to their target membrane. Although, the general concepts of membrane protein targeting and insertion have been deciphered, there are still significant gaps in our understanding on how these targeting machineries handle the large diversity of membrane proteins.

Employing a wide range of biochemical, biophysical and in vivo methods we want to determine how membrane proteins are targeted to and integrated into the cytoplasmic membrane of prokaryotic cells. In a first project, we will study the dynamic assembly of protein transport channels by in vivo and in vitro crosslinking combined with mass spectrometry. The second project will explore non-canonical protein targeting pathways by single-molecule imaging and biochemical assays.

We are looking for highly motivated applicants with a Master’s degree in life sciences and a strong background in Microbiology/Cell Biology and Biochemistry. Project 1 requires experience with membrane protein expression and purification. Project 2 requires experience with RNA and some background in quantitative biology and Biophysics. Very good knowledge in English is required for both projects.

We are an international and highly motivated research team, working in a very attractive scientific environment and in one of the most beautiful parts of Germany. We offer intense training both at the practical and theoretical level and encourage students to present their data at national and international meetings. Assistance in moving to Freiburg is also provided.

We are looking forward to receive your application including a motivation letter, your CV, records of your Bachelor and Master studies with the important certificates and two letters of recommendation via email until January 20th 2019. Informal inquiries via Email about the position are welcome.

Methoden: in vitro transcription/translation assays; site-directed cross-linking; membrane protein purification; fluorescence microscopy and single molecule imaging; isotope labeling of proteins, RNA analyses, mass spectrometry
Anfangsdatum: 15. Februar 2019
Geschätzte Dauer: 3-4 Jahre
Bezahlung: TVL-E13 65%
Papers: Kuhn, P., Draycheva, A., Vogt, A., Petriman, N.A., Sturm, L., Drepper, F., Warscheid, B., Wintermeyer, W., and Koch, H.G. (2015) Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. J. Cell Biol. 211, 91-104

David Braig, Tracy L. Nero, Hans-Georg Koch, Benedict Kaiser, Xiaowei Wang, Jan R. Thiele, Craig Morton, Johannes Zeller, Jurij Kiefer, Lawrence A.Potempa, Natalie A. Mellett, Luke A. Miles, Xiao-Jun Du, Peter J. Meikle, Markus Huber-Lang, G. Björn Stark, Michael W. Parker, Karlheinz Peter, Steffen U. Eisenhardt (2017) Transitional changes in the CRP structure lead to the exposure of pro-inflammatory binding sites. Nature communications 8, 14188

Denks, K., Sliwinski, N., Erichsen, V., Borodkina, B., Origi, A. and Koch, H.G. (2017) The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel Nature Microbiology, 2, 16265

Sachelaru, I., Winter, L., Knyazev, D., Zimmermann, M., Vogt, A., Kuttner, R., Ollinger, N., Siligan, C., Pohl, P. and Koch, H.G. (2017) YidC and SecYEG form a heterotetrameric protein translocation channel. Scientific reports 7, 101