“This is one of the best times to do science”
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.
Close friends and distant relatives
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.
PETISCO - a multi-tool for piRNA processing
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.
Proteus changes his Akt
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.
Tardigrades take the stage
Discussions with his family about science inspired Adrià Nogales Moral from the lab of Alwin Köhler to become involved in communicating science to a wider audience. He has recently been awarded an Impact Award by the University of Vienna, which he will use to increase the visibility of his research on tardigrades, the most resilient organisms on earth. The award is financed by the City of Vienna and given to outstanding dissertation projects with the potential to reach target groups outside the scientific community and to add social, cultural or economic value.
Getting out of your comfort zone
Nathan Palmer, a postdoc in the Matos lab, has been awarded an EMBO Postdoctoral Fellowship that supports internationally mobile postdoctoral researchers. We talked to him about his work and the importance of international experience.
Signal transduction: In the right place, at the right time
Cells integrate internal and external stimuli through complex signaling pathways in order to adapt to changing environments. In particular, cells must know when to grow and when not to. In the phosphoinositide 3-kinase (PI3K) pathway downstream of growth factors, Sgk3 is activated by the signaling lipid PI3P, but the precise mechanism of its activation is unknown. In work published in the Journal of Biological Chemistry, the lab of Thomas Leonard has discovered that Sgk3 is locally activated on membranes by PI3P. In the absence of PI3P, its membrane binding domain maintains Sgk3 in an inactive conformation. Since Sgk3 is upregulated in some cancers, its autoinhibited conformation represents a novel therapeutic target.
Max Perutz PhD Fellowships awarded
Luis Miguel Cerron Alvan and Helena Bragulat Teixidor have been selected as the first Max Perutz PhD Fellows. The program was established earlier this year with the goal to reward the most ambitious and innovative PhD projects at the institute.
Hot off the press: a new role for histone modifications in genomic imprinting
Imprinted genes are expressed from either the paternal or maternal allele. Reporting in Nature Communications, scientists led by Martin Leeb have now discovered 71 previously unrecognized imprinted genes in preimplantation blastocysts. The study found that imprinting created by differential histone marks plays a more prominent role in the preimplantation blastocyst than canonical DNA methylation mechanisms.
ÖAW DOC Fellowships for Max Perutz Labs students
The Austrian Academy of Sciences (ÖAW) has awarded four DOC fellowships to Max Perutz Labs PhD students Dana Abdeen, Aleksandra Anisimova, Daria Filipczak, and Helena Bragulat Teixidor. The DOC program offers funding for highly qualified doctoral candidates in all areas of research. The fellowships amount to 38,000 Euros each and will support the young researchers’ work, spanning from meiosis, lamins, inter-organelle communication, and protein quality control.
Meiosis: Mind the gap
Meiosis is a specialized cell division process required to generate gametes, the reproductive cells of an organism. During meiosis, paternal and maternal chromosomes duplicate, pair, and exchange parts of their DNA in a process called meiotic recombination. In order to mediate this exchange of genetic material, cells introduce double strand breaks (DSBs) into their chromosomal DNA. Scientists from the lab of Franz Klein from the Department of Chromosome Biology at the Max Perutz Labs, a joint venture of the University of Vienna and the Medical University of Vienna, have now discovered that cells sometimes liberate DNA fragments at sites of paired, or double, DSBs. Whilst this presents an obvious risk of germline mutations as a consequence of erroneous repair or of integration of fragments from elsewhere at break sites, it may also be a source of evolutionary diversity. The study is published as a research article in Nature.
Two Max Perutz Labs scientists elected as EMBO members
Every year EMBO (European Molecular Biology Organization) selects distinguished scientists who have made outstanding contributions in the field of the life sciences. New members are elected by peers based on individual recommendations by renowned researchers in their respective field. Kristin Tessmar-Raible and Alwin Köhler have joined the EMBO community.
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