PhD in molecular biology (Germany) ~

19 de julio de 2014

PhD in molecular biology (Germany)

We offer: The Institute ( offers the opportunity to work in an interactive and dynamic setting, is equipped with state-of-the-art facilities and well funded. We provide a creative working atmosphere and have active exchange programs with many scientists abroad.

This project will investigate the molecular mechanisms and physiological consequences of chromatin recruitment of the serine/threonine kinase HIPK2 . We have already performed ChIP-Seq experiments and found that HIPK2 binding motifs have a prominent overlap with DNA motifs for a zinc finger transcription factor, suggesting that this transcription factor functions as a docking port for the kinase. It is thus planned to measure chromatin association of HIPK2 or the transcription factor after shRNA-mediated depletion of the respective interaction partner. It will also be important to determine the effects of transcription factor and/or HIPK2 depletion on mRNA expression of their target genes by RT-qPCR. The transcription factor and HIPK2 share a number of common binding partners, therefore it will be interesting to reveal whether these partners also occur at the genomic loci containing the transcription factor/HIPK2 complex. In addition we will use the CRISPR-Cas system to remo!
 ve prototypic genomic HIPK2/transcription factor binding sites, followed by the analysis of HIPK2 and transcription factor chromatin recruitment by ChIP experiments. A variety of different methods will be employed to understand the mechanisms and physiological consequences of HIPK2 chromatin recruitment.

Your profile: You have succesfully finished your Master or equivalent degree. You are highly self-motivated and ambitious and can work well in a highly active international research team, but also work on your own. Participation in the running  teaching program is expected.

The university is an equal opportunity employer, and applications from women or candidates with children are encouraged. Applications of severely disabled with same suitability are preferred. Application deadline is end of July 2014.

Please send your CV, two names of reference and the further usual documents to

Prof. M.L. Schmitz
Biochemical Institute
Friedrichstrasse 24
35392 Giessen (Germany)

We would appreciate your sending the application papers in copy, since we are not going to send your papers back once the application procedure is going to be finished.

ChIP, qPCR, immunofluorescence, clong, CRISPR, RNA seq, biochemistry

Anfangsdatum: 12. Juli 2014

geschätzte Dauer: 36 months

Bezahlung: A13/2

1) Calzado,M.A., de la Vega,L., Möller,A., Bowtell,D.L., and Schmitz,M.L. (2009). An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response. Nature Cell Biol. 11, 85-91.
2) Geng,H., Wittwer,T., Dittrich-Breiholz,O., Kracht,M., and Schmitz,M.L. (2009). Phosphorylation of NF-kB p65 at serine 468 controls its COMMD1-dependent ubiquitination and target gene specific proteasomal elimination. EMBO Rep. 10, 381-386.
3) Renner,F., Moreno,R., and Schmitz,M.L. (2010). SUMOylation-dependent localization of IKKe in PML nuclear bodies is essential for protection against DNA damage-triggered cell death. Mol. Cell 37, 503-515.
4) Ritterhoff,S., Farah,C.M., Grabitzki,J., Lochnit,G., Skurat,A.V., and Schmitz,M.L. (2010). The WD40 repeat protein Han11 functions as a scaffold protein to control HIPK2 and MEKK1 kinase functions. EMBO J. 29, 3747-3749.
5) de la Vega,L., Grishina,I., Moreno,R., Krüger,M., Braun,T., and Schmitz,M.L. (2012). A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress. Mol. Cell 46, 472-483.
6) Saul,V.V., de la Vega,L., Milanovic,M., Krüger,M., Braun,T., Fritz-Wolf,K., Becker,K., and Schmitz,M.L. (2013). HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop. J. Mol. Cell Biol. 5, 27-38.
7) de la Vega,L., Hornung,J., Kremmer,E., Milanovic,M., and Schmitz,M.L. (2013). Homeodomain interacting protein kinase 2-dependent repression of myogenic differentiation is relieved by its caspase-mediated cleavage. Nucleic Acids Res. 41, 5731-5745.
8) Handschick,K., Beuerlein,K., Jurida,L., Bartkuhn,M., Müller,H., Soelch,J., Weber,A., Dittrich-Breiholz,O. Schneider,H., Scharfe,M., Jarek,M., Stellzig,J., Schmitz,M.L., and Kracht,M. (2014). Cyclin-dependent kinase 6 is a chromatin-bound cofactor for NF-kB-dependent gene expression. Mol. Cell 53, 193-208.

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