Finally, our method to purify RNA-binding proteins in yeast is out! The research paper in Methods gives a complete overview over all steps of the interactome capture approach and provides a comprehensive discussion on the background.
The article is open access (CC-BY license) and will have a pubmed link soon.
Temporary location: here.
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
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.
There is an interesting opening for a postdoctoral position at the DKFZ in Heidelberg: Cancer, RNA and metabolism at the Galy lab!
Our colleague Bruno Galy (DFKZ Heidelberg, Germany) has a job opportunity for a PhD student to work at the interface of cellular metabolism and cancer.
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!
Senthil joined our group as postdoctoral fellow. He received a fellowship from the IRI to study outer membrane vesicles of bacterial pathogens and the role of exosomes during infection processes.
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 🙂
The research group of Bruno Galy is searching for a PhD student with an interest in cancer research and metabolism.
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