We will advertise soon an MRC-funded postdoctoral position. The goal will be to determine the scope of RBPs employed by viruses and will involve state-of-the-art RNA biology and virology methods as well as next generation proteomics and RNAseq. If you want to get more information, please, feel free to contact us.
Our colleague Bruno Galy offers a postdoc position in the field of ‘Cancer Metabolism’ to work at the ‘Virus-associated carcinogenesis’ division in the DKFZ, Heidelberg, Germany.
One major interest of the Galy lab is iron metabolism. Iron is a trace element important for a plethora of cellular functions and like other metabolic pathways, iron homeostatic mechanisms are frequently altered in cancer. Using a combination of biochemical and molecular biology assays together with state-‐of-‐the-‐art mouse models and organoid cultures, the candidate will study the function of central regulatory systems of iron homeostasis in various aspects of tumorigenesis, with a strong focus on hepatic and intestinal cancer. The successful applicant will more specifically investigate the impact of local iron mismanagement in cancerous cells versus cells of the tumor microenvironment on the inflammatory processes that lead to carcinoma formation.
To inquire about the position, the job profile, and the conditions, contact Dr. Bruno Galy.
Our last review was recently published in Nature Reviews – Molecular and Cell Biology. We discuss about the recurrent identification of unorthodox RBPs by proteome-wide methods to identify proteins bound to RNA, and discuss about the potential biological meaning of this exciting discovery.
What can we expect from the discovery of so many new RBPs? Some might side with Miranda from Shakespeare’s The Tempest and marvel at these novel and goodly RBPs that populate the RNA interactome. Others might think of Huxley’s brave new world and fear dystopia, considering the newly discovered RBPs as nonconformist misfits lacking biological function. Which roles do these new RBPs play?
Hentze MW, Castello A, Schwarzl T, Preiss T.
RBDmap employs UV crosslinking, oligo(dT) selection, partial proteolysis and quantitative proteomics to identify the protein regions engaged in RNA binding in a system-wide scale. Applied to HeLa cells it reported 1,174 RNA-binding sites mapping to 529 RBPs, many of which lacking known RNA-binding domains. A detail RBDmap protocol has now been released for the community in Nature protocols
“The use of RBDmap can now be extended to other cell lines or organisms and can be used to profile in a global scale the behaviour of RNA-binding domains in response to different physiological conditions and stresses.”
Identification of RNA-binding domains of RNA-binding proteins in cultured cells on a system-wide scale with RBDmap. Castello A, Frese CK, Fischer B, Järvelin AI, Horos R, Alleaume AM, Foehr S, Curk T, Krijgsveld J, Hentze MW. Nat Protoc. 2017 Dec;12(12):2447-2464. doi: 10.1038/nprot.2017.106. Epub 2017 Nov 2. PMID: 29095441