After 15 successful years, FWF funding of our Doctoral School in RNA Biology (DK RNA-Biologie, https://www.phd-rna-biology.at) comes to an end. Therefore, we would like to invite all people involved to celebrate this long-lasting support of the Viennese RNA community with the "Vienna RNA Meeting 2021".
It is the highlight of a series of architectural changes at the Perutz: The Max Bar on the Roof has opened its doors.
Stefan Ameres obtained his Master’s degree from the University of Erlangen-Nuremberg (Germany) and his PhD from the University of Vienna. After postdoctoral training in the United States at the University of Massachusetts Medical School he joined the Institute of Molecular Biotechnology in Vienna as a group leader in 2012. In 2020 he was appointed Professor of RNA Biology at the Max Perutz Labs, University of Vienna. We talked to him about why RNA is the molecule of (his) life, how he rocked the terrace of the Perutz with his band as a PhD student, and what his advice to young researchers is.
In order to exchange genetic material between parental chromosomes during meiosis, cells need to introduce DNA double strand breaks (DSBs) that are later repaired in a specific manner. Which proteins are necessary and sufficient for this process and how they achieve faithful DSB formation and repair is still poorly understood. The lab of Peter Schlögelhofer and their collaborator Mathilde Grelon from the INRAE (Versailles, France) have systematically investigated the interactions between DSB proteins in the model plant Arabidopsis thaliana. Their work also identified a key protein that links the DSB complex to the DNA repair machinery. The study is published in Nucleic Acids Research.
Piwi-interacting RNAs (piRNAs) are essential to repress transposable elements in the animal germline. In the nematode worm C. elegans, piRNA biogenesis requires a protein complex called PETISCO, but exactly what PETISCO does and how it works is poorly understood. The group of Sebastian Falk and their collaborators now provide unique insights into the molecular details of piRNA processing in C. elegans. PETISCO also has a second, unknown function in embryogenesis, which is dependent on the binding of a different accessory protein. The work resolves the question of how one protein complex can fulfill two different functions and is expected to help elucidate the elusive role of PETISCO in early development. The study is published in Genes & Development.
The protein kinase Akt is activated in the PI3K pathway by a combination of signaling phospholipids and phosphorylation by upstream protein kinases. However, their respective contributions to the activity of Akt in the cell remains controversial. The lab of Thomas Leonard has determined the first high-resolution structure of near full-length Akt1 without the use of pharmacological inhibitors. Their findings provide new insights into how signaling lipids limit the spatial activity of Akt to membranes. The study, published in PNAS, also reveals the mechanistic basis of how Akt is perturbed in cancer and in Proteus syndrome, a rare overgrowth disease.
The Max Perutz Labs are embedded in the Vienna BioCenter, providing access to outstanding core facilities shared by all members of the campus in addition to facilities unique to our institute.
With a strong molecular focus and a diversity of model organisms, we aim to bridge basic research with biomedicine.
To honour an extraordinary teacher and scientist, the Max Perutz Labs were named after Max Ferdinand Perutz, who, together with John C. Kendrew, was awarded the 1962 Nobel Prize in Chemistry for his studies on the structure of globular proteins ...
The Max Perutz Labs seek to educate students to think critically and analytically, challenge them to set ambitious goals, and instill in them both broad horizons and deep understanding. In doing so, we aspire to furnish them with the necessary knowledge and skills to push forward the frontiers of 21st century biomedical science.