Postdoc Anete Romanauska from Köhler lab has been awarded the Denise M. Barlow Award for "Best Thesis on Biological Mechanisms". After the Weintraub Award and the Vienna BioCenter PhD Award this marks the third distinction for Anete’s PhD research on lipid metabolism in the nucleus. The prize is named after molecular biologist Denise P. Barlow and recognizes academic talent among the four research institutes she was associated with: The Max Perutz Labs, the Institute of Molecular Biotechnology (IMBA), the Research Institute of Molecular Pathology (IMP), and the Research Center for Molecular Medicine of the Austrian Academy of Sciences (CeMM). Its aim is to honor exceptional PhD work with an emphasis on novel biological mechanisms, something Denise P. Barlow was fond of.
Oxidative stress is a biochemical condition in which the levels of oxidant molecules exceed the level of reductants (also known as anti-oxidants) in an organism. High concentrations of oxidants can alter the activity of enzymes and damage lipids, proteins and nucleic acids. Reporting in Molecular Cell, the lab of Javier Martinez reveals a novel and surprising mechanism of how an essential enzyme protects itself from oxidative stress. The tRNA ligase RTCB evolved with another protein whose sole purpose is to protect RTCB from oxidation. This protein, called PYROXD1, is linked to myopathies in humans and, paradoxically, uses a key cellular oxidant, NADP+, to protect its partner.
During germ cell development faulty meiocytes are eliminated via apoptosis, a programmed cell death to ensure that only healthy gametes are produced. The lab of Verena Jantsch has now discovered a previously undescribed role for topoisomerase 3 (TOP-3) in oocyte quality control of the model organism C. elegans. In the absence of TOP-3, cells accumulate aberrant recombination intermediates in the pre-meiotic and meiotic compartments of the gonad that are less capable of triggering apoptosis. DNA repair is directed to less accurate pathways, resulting in a pool of oocytes with low quality. The study is published in the Journal of Cell Biology.
The Medical University of Vienna in cooperation with the University of Vienna has launched a new Master´s Program in Molecular Precision Medicine dedicated to an understanding of human pathogenesis and the treatment of disease at a molecular and mechanistic level. The course brings basic, translational, and clinical scientists together with doctors to educate students in the opportunities, challenges, and future perspectives of precision medicine.
Centrioles are surrounded by a dense meshwork of proteins called the pericentriolar material (PCM), which together form centrosomes, the main microtubule-organizing centers of the cell. Alexander Dammermann’s group has discovered that centrosomes persist without centrioles in post-mitotic neurons of C. elegans. Key components of the PCM are expressed and incorporated into these centrosomes independent of centrioles and known mitotic regulators. The study, published in Current Biology, suggests that the assembly and maintenance of mitotic and non-mitotic centrosomes may be different.
The Austrian Science Fund has granted a doc.fund to a group of researchers from the Max Perutz Labs, the Faculty of Physics of the University of Vienna, the IMP and the IMBA. The grant is endowed with 1,6 Million Euros and will fund eight PhD positions over four years. Students will be recruited via the Vienna BioCenter PhD Program, and will receive multidisciplinary training to tackle fundamental questions in the field of liquid-liquid phase separation in biology. The doc.fund expects to start recruiting in fall 2021, and is coordinated by Bojan Zagrovic, a computational biologist at the Max Perutz Labs.
Lamins are structural proteins found at the nuclear periphery, where they regulate the mechanical properties of the nucleus and the organization of genetic material within the nucleus. However, they also play a poorly understood role in the nucleoplasm. New work from the lab of Roland Foisner and their collaborators from the Bar Ilan University (Israel) now shows that binding of A-type lamins in the nuclear interior to a protein called LAP2α regulates their mobility and that of surrounding chromatin. The study is published in e-life.