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PhD position (m/f)


PhD positions (65 %) available at the Department of Internal Medicine I (Krehl-Klinik).

PI: Dr. Jens Tyedmers

Project Title: Amyloid Aggregate Sorting in Yeast

Application deadline: June 30, 2017

Start of PhD project: August 2017

Source of funding: DFG (36 month)

Project description and Methods

The formation of protein aggregates including amyloids is a hallmark of several fatal diseases. A commonly employed model organism to study protein aggregation, Saccharomyces cerevisiae, possesses at least three independent Protein Quality Control Sites (PQC’s) where different types of aggregates are deposited. The group of J. Tyedmers studies one of these deposition sites termed "Insoluble Protein Deposit (IPOD)" and has most recently discovered that amyloid aggregates are recruited to the IPOD via vesicular transport along actin tracks. The project aims 1) to characterize the molecular composition of this novel recruitment machinery, 2) to determine the physiological role of the IPOD and its influence on cellular homeostasis, 3) to study the fate of aggregates deposited at the IPOD.

Methods that will be used:

  • general yeast genetics methods
  • standard molecular biology techniques
  • fluorescence microscopy
  • Screening with yeast libraries
  • Flow Cytometry
  • FACS-based isolation strategies for aggregates
References
  • Kumar R, Nawroth P, Tyedmers J. Prion Aggregates are recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-based vesicular transport. PLoS Genet. 2016 Sep 30;12(9):e1006324.
  • Hernandez-Hidalgo I, Fleming T, Eckstein V, Herzig S, Nawroth P, Tyedmers J. Characterization of Aggregate Load & Pattern in living Yeast Cells by Flow Cytometry. Biotechniques. 2016 Sep 1;61(3):137-48.
  • Tyedmers J. Patterns of [PSI+] aggregation allow insights into cellular organization of yeast prion aggregates. Prion. 2012 Jul 1;6(3):191-200.
  • Tyedmers J, Mogk, A & Bukau, B. Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol. 2010 Nov;11(11):777-88.
Required Qualifications

We are looking for a highly motivated and communicative Ph.D. student (m/f) who is interested to perform competitive high quality scientific research in the area of protein misfolding and aggregation. She or he will have a Masters Degree in Life sciences acceptable to HBIGS and a strong background in molecular biology and/or cell biology. Previous experience in working with yeast, High-throughput screening and/or Flow Cytometry would be an advantage.

Contact & Application

Successful candidates are expected to apply for membership at the HBIGS Graduate School (http://www.hbigs.uni-heidelberg.de/).

Applications can be send directly to j.tyedmers@zmbh.uni-heidelberg.de or via the HBIGS application system (http://www.hbigs.uni-heidelberg.de/) , position “Bukau_Tyedmers”.



Universitätsklinikum Heidelberg
Zentrum für Innere Medizin
Klinik für Endokrinologie, Stoffwechsel und Klinische Chemie (Innere Medizin I)
Im Neuenheimer Feld 410
69120 Heidelberg

Publishing date: May 24, 2017

Wir stehen für Chancengleichheit. Schwerbehinderte werden bei gleicher Eignung vorrangig eingestellt. Das Universitätsklinikum strebt eine generelle Erhöhung des Frauenanteils in allen Bereichen und Positionen an, in denen Frauen unterrepräsentiert sind. Qualifizierte Frauen sind daher besonders aufgefordert, sich zu bewerben. Vollzeitstellen sind grundsätzlich teilbar, soweit dienstliche oder rechtliche Gründe nicht entgegenstehen.

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