Ruprecht-Karls-Universität Heidelberg
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Sinning0219 - Scientist (f/m) / PhD position
Project no:

Project leader:

Project supervisor:
Sinning, Irmgard
Application deadline:
15. Apr 2019
Start of PhD project:
1. May 2019

Project description:

Impact of co-translational protein folding on protein homeostasis
Research in our group centers around cotranslational processes that occur at the ribosomal tunnel exit. Here, a rather larger number of proteins and complexes comprising chaperones, enzymes and targeting factors seem to compete for access to the nascent chain. The ribosome associated complex (RAC) and its Hsp70 partner Ssb form a unique chaperone triad at the ribosome. Having recently solved the first structures of RAC and Ssb, and after dissection the ribosome interaction of Ssb, we are now interested in the mechanistic details of how RAC and Ssb mediate the substrate interaction and handover at the ribosome. We combine an integrated structural biology approach (using X-ray crystallography, cryo-EM, SAXS and NMR) with in vivo and in vitro analyses of these chaperones in yeast and other organisms. Our work is interdisciplinary and will allow the talented PhD student to gain expertise in a broad range of structural, biophysical and biochemical methods. At the end, we will obtain mechanistic insights into the workings of a central co-translational chaperone machinery.
1. Gumiero, A., Conz, C., et al. & Sinning, I. (2016) Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain, Nat. Comms. 7: 13563.

2. Weyer, F. A., Gumiero, A., Valentín Gesé, G., Lapouge, K. & Sinning, I. (2017) Structural insights into a unique Hsp70/Hsp40 interaction in the eukaryotic ribosome-associated complex, Nat. Struct. Mol. Biol. 24: 144-151.

3. Zhang, Y., Sinning, I. & Rospert, S. (2017) Two chaperones locked in an embrace: Structure and function of the ribosome-associated complex RAC, Nat. Struct. Mol. Biol. 24: 611-619.
Methods that will be used:
Integrated structural biology: X-ray crystallography, cryo-EM, SAXS and NMR, as well as in vivo and in vitro analyses using biochemical and biophysical techniques, protein expression and purification, protein-protein interactions.
Cooperation partners:
Personal qualifications:
The candidate should have a strong background in biochemistry/biophysics with a specific interest in structural biology. The candidate should be highly motivated to succeed in science. Experience in protein expression and purification would be an advantage.