Research update: Review on the expanding universe of ribonucleoproteins

RNA-protein interactions have been studied intensively in recent years. Particularly novel methods such as mRNA interactome capture led to discovery of hundreds of novel RNA-binding proteins (RBPs). However, many of these recently identified RBPs lack classical RNA-binding domains.

In our review The expanding universe of ribonucleoproteins: of novel RNA-binding proteins and unconventional interactions, we discuss features of RNA-protein interactions and propose a more RNA-centric view: maybe RNA evolved to bind certain proteins rather than vice versa?


The article is open access and available here: Pflügers Archiv – European Journal of Physiology (2016)

or here: pubmed link


Bachelor student invasion!

We are proud to host two Bachelor students who are conducting their final thesis in our lab.



Victoria Riebe (BSc Biology) is working on CRISPR/Cas9 in bacteria.



Valentina Tovazzi (BSc Biophysics) is testing Salmonella proteins for RNA-binding activity.

Goodbye Tobias!

Todays is Tobias’ last day in the lab. As part of his Master studies in Molecular Life Sciences at the Humboldt-Universität zu Berlin, he did a 6 month internship (so called Projektmodul) in our group. Tobias worked on the purification of tagged mutant versions of the protein Cas9 from Streptococcus pyogenes which is a key enzyme of the famous CRISPR system.


We will miss him in our team and wish all the best for his further studies!




From left: Benedikt, Senthil, Julie, Davide. Missing in the picture: Erika, Tobias.

Its thursday, Feb. 4th 2016 11:11 am and we tried to celebrate Karneval in Berlin. What other place to go here than the “Ständige Vertretung?” Unfortunately, we were all but alone 🙂

Research update: evolutionary conserved RNA-binding proteins

During the last years, hundreds of novel RNA-binding proteins (RBPs) have been detected in mammalian cell lines. Now, we mapped the mRNA-bound proteome of a complete organism: the yeast S. cerevisiae. Additionally, we determined the mRNA interactome of human hepatocytic cells (HuH-7).

Having comprehensive information on RBPs from a eukaryotic single cell organism and from mammalian cell lines, we defined a conserved core mRNA interactome of eukaryotic mRNA-binders. The core consists of many well-established RNA-binding proteins but also of many enzymes from diverse biochemical pathways and glycolysis emerges as hot-spot of conserved RBPs.

We also identified another interesting difference among some conserved eukaryotic RBPs in their overall RNA-binding architecture: throughout evolution, a steady increase in the repetition of short amino acid tripeptide motifs in unstructured regions of proteins could be observed.


Beckmann BM, Horos R, Fischer B, Castello A, Eichelbaum K, Alleaume A-M, Schwarzl T, Curk T, Foehr S, Huber W, Krijgsveld J & Hentze MW.  The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs. Nature Communications (2015); 6:10127