Update! Watch the recording of this talk (edited to remove unpublished data that was presented on the live event).
This talk is an activity from the FEBS Junior Section, an initiative set up by students and young researchers from some of the FEBS Constituent Societies. Each month a Junior Section from one of the participant Societies organizes an online event on either a research or a career topic. This January talk is organised by Junior-GBM, the junior section of the GBM.
Want to join this platform for young European life scientists? Learn more about our initiative, check out the Room for the FEBS Junior Section and – if you do not have a junior section yet – read this post about how to set one up!
Speaker: Dr. Andreas Schlundt, Goethe University Frankfurt, Germany
Topic: “The roles of sequence, structure and dynamics for specific RNA-recognition by proteins.”
Time: 13 January 2022, 19:00 (CET)
For more information, see the presentation abstract below and visit the Schlundt lab website.
Specific and highly-organized interactions between RNA and proteins are present at many stages of cellular processes, but most prominently occur between mRNAs and RNA-binding proteins (RBPs) on the post-transcriptional level. Here, proteins act to regulate levels of mRNAs either by promoting or inhibiting their degradation and thereby actively steering gene expression. A misbalanced level of mRNAs in fact can account for severe diseases like autoimmunity and cancers. RNA-protein interactions have very recently moved yet more into focus with the appearance of SARS-CoV-2, a positive-sense single-stranded RNA virus, which causes the devastating Covid-19 disease. The virus exploits a multitude of interactions with its own and host proteins as the basis for its efficient replication and progression.
A common challenge in literally all RNA-protein complexes is to understand their basis for specificity. It turns out that specificity is governed by sequence and molecular fold. Yet, there is growing evidence for a particular role of dynamics within both RNA and proteins to achieve specificity. Affinity on the other hand is often governed by multimodal interactions, i.e. proteins use more than one RNA-binding domain for their engagement with RNAs.
It is our central objective to disentangle relevant RNA-protein interactions both in human cells as well as e.g. in the SARS-CoV-2 virus. We seek to understand the respective bases for selectivity in order to derive rules for their existence in biological systems. In this frame, we rely on high-resolution structural data as e.g. obtained from crystallography. Further, we put a particular emphasis on the role of dynamics and flexibility within those systems, which can perfectly be achieved with solution techniques like Nuclear Magnetic Resonance (NMR) spectroscopy or Small Angle X-ray Scattering (SAXS). In this talk, I will give an overview of selected topics where we apply a combination of methods to investigate human mRNA-regulation and viral RNA and protein components as addressable drug targets. I will in particular stress out the role of local infrastructure and collaborative networking for our efforts.