The Falk Lab studies various mechanistic aspects of nuclear RNA Metabolism using a biochemical approach focusing on structural biology (X-ray crystallography and Cryo-EM). We recently discovered a new factor that is involved in RNA surveillance in human cells. We find that this new factor interacts with other elements from the transcription, splicing, and RNA degradation machinery. To unravel this new factor's molecular function, we apply a multidisciplinary biochemical, cell biological, and structural biological approach. We are looking for a master student with a genuine interest in advanced protein biochemistry methods.
We are a small team and offer extensive training in molecular biology, biochemistry, and structural biology, with the possibility to conduct cutting edge research.
For further information, please visit our homepage or contact Sebastian by email.
Requirements: Finished study (B. Sc.) in Molecular Biology, Biochemistry or related, 45 ECTS accomplished in the Master module
Duration: ca. 12 months
Payment: acc. to FWF rates
Max Perutz Labs
Dept. of Structural and Computational Biology, Univ. Wien Rm. 1622, Campus Vienna Biocenter 5, A-1030 Wien
Lingaraju, M., Johnsen, D., Schlundt, A., Langer, L.M., Basquin, J., Sattler, M., Jensen, T.H., Falk, S.* and Conti, E.* (2019). The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs. Nature Communications 10, 3393
Schuller, J.M.*, Falk, S.*, Fromm, L., Hurt, E. and Conti, E. (2018). Structure of the nuclear exosome captured on a maturing pre-ribosome. Science Apr 13; 360, 219-222
Falk, S., Ebert, J., Kögel, A, Bonneau, F. and Conti, E. (2017). Mpp6 incorporation into the nuclear exosome contributes to RNA channeling through the Mtr4 helicase. Cell Reports 20, 2279–2286.