Helmholtz Zentrum München Deutsches Forschungszentrum für Gesundheit und Umwelt

Project description

The Schneider group wants to unravel how epigenetic mechanisms control genome function by applying different biochemical and biophysical approaches as well as various mouse and disease models.
Our group has a strong experience in deciphering the function of novel types and sites of histone modifications and their role in cancer and metabolic diseases (see for examples: Tropberger et al., Cell 2013; di Cerbo et al., eLife 2014; Kebede et al., NSMB 2017). For the future we want to identify novel pathways regulating genome function and in particular their deregulation in cancer or diabetes. This will allow us to discover new therapy targets and unique diagnostic or prognostic markers.

For a novel project on the interphase between chromatin biochemistry, epitranscriptomics (RNA modifications) and epigenetics we are looking for a PhD student with previous lab experience in e.g. chromatin/transcription research. The PhD student will undertake a challenging project, the study of a new covalent modification, in an internationally renowned environment. The aims of the project are to i) map the modification for the first time, ii) to identify the modifying pathways (writers and erasers), iii) to unravel the function of the modification in tissue culture and mouse models as well as iv) the consequences of its deregulation in different cancer models.

This project will address a central question in epigenetics: what are the mechanisms via which the cellular environment controls genome function and the transcriptome? You will be part of a very enthusiastic and international team, learn state of the art technologies (e.g. imaging techniques, Crispr/Cas9 approaches,  or different types of omics such as: RNAseq, ChIPseq, Cut&Run, MeRIP, ATACseq…) and will have the possibility to advance the fascinating fields of epigenetics and epitranscriptomics.



Related literature

  • Tropberger et al (2013). Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer. Cell. 152(4):859-72.

  • Di Cerbo et al (2014). Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription. eLife 2014;3:e01632.

  • Kabede AF et al (2017). Histone propionylation is a mark of active chromatin. Nat Struct Mol Biol. 24(12):1048-1056.