Characterization of telomere binding proteins

Scientific Background

Telomeres are nucleoprotein structures at the ends of linear chromosomes and present an essential feature for genome integrity. Our group uses modern technology and molecular biology techniques to identify and characterize novel telomeric proteins in diverse species. Using a quantitative interactomics screen based on quantitative mass spectrometry with telomeric DNA used as a bait, we identified several new telomeric proteins in the last years. For example, we characterized the telomere length regulators HOT1 (Kappei*, Butter* et al., EMBO J 2013) and ZBTB48 (Jahn*, Rane* et al., EMBO Rep 2017) as well as the ALT-specific telomere binding protein ZBTB10 (Bluhm et al., Nucleic Acids Res 2019) in mammals. Furthermore, we conducted a phylointeractomics screen to study putative telomere-associated proteins from fish to mammals (Kappei*, Scheibe* et al., Nat Commun 2017). In the future, we want to deepen our understanding of the function of our previously reported telomere-binding proteins and are in the process of developing zebrafish lines. Additionally, we also applied our techniques to characterize novel telomeric proteins in other species such as trypanosomes (Reis et al., 2018), S. pombe and C. elegans (Dietz*, Almeida* et al., BioRxiv 2020).

The Project

We are looking for a Postdoc with prior experience in telomere biology and a special interest in techniques that can be generically applied to characterize telomere-associated proteins in eukaryotic species. We are currently characterizing telomere-binding proteins in cell culture and using zebrafish, C. elegans and S. pombe as model organisms. You will perform molecular biology, biochemistry and cell culture to characterize telomere binding proteins. To characterize novel candidates, we will also employ unbiased quantitative techniques such as RNA-Seq, quantitative proteomics and ChIP-Seq. While support in bioinformatics is available, expertise in molecular biology is required.

Required Qualifications

  • PhD in a relevant field
  • Fluent in English (spoken and written)
  • Prior experience in telomere biology
  • Expertise in molecular biology

Publications Relevant to the Project

(*indicates joint contribution, #indicates joint correspondence)

Dietz S.*, Almeida M.*, Nischwitz E., Schreier J., Viceconte N., Fradera Sola A., Renz C., Ceron Noriega A., Ulrich H.D., Kappei D., Ketting R.F. and Butter F (2020) The two paralogs TeBP1 and TeBP2 are telomeric double strand binders in C. elegans.

Bluhm A, Viceconte N, Li F, Rane G, Ritz S, Wang S, Levin M, Shi Y, Kappei D and Butter F (2019) ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2. Nucleic Acids Res, 47:1896–1907

Jahn A*, Rane G*, Paszkowski‐Rogacz M, Sayols S, Bluhm A, Han C, Draškovič I, Londoño‐Vallejo JA, Kumar AP, Buchholz F#, Butter F# and Kappei D# (2017) ZBTB48 is both a vertebrate telomere‐binding protein and a transcriptional activator. EMBO Rep, 18:929–946

Kappei D*, Scheibe M*, Paszkowski-Rogacz M, Bluhm A, Gossmann TI, Dietz S, Dejung M, Herlyn H, Buchholz F#, Mann M# and Butter F# (2017) Phylointeractomics reconstructs functional evolution of protein binding. Nat Commun, 8:14334

Kappei D*, Butter F*, Benda C, Scheibe M, Draškovič I, Stevense M, Novo CL, Basquin C, Araki M, Araki K, Krastev DB, Kittler R, Jessberger R, Londoño-Vallejo JA, Mann M and Buchholz F (2013) HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment. EMBO J, 32:1681–1701 (*indicates joint contribution)

More details

Dr Falk Butter

Research website