Eukaryotic messenger ribonucleoprotein (mRNP) particles are the functional entities that carry genetic information to the protein synthesizing machinery. These ribonucleoprotein complexes are dynamic and diverse, as highlighted by the copious number of proteins and transcripts identified in global proteomic and transcriptomic studies. However, little is known about the composition and architecture of individual mRNPs, and how changes in mRNP structure relate to their function or to dysfunction. The GOVERNA project will address this gap in knowledge by purifying specific mRNPs and delving into their molecular and structural arrangement. With our preliminary data serving as a springboard, the project combines genomic tagging engineered to maintain the most physiologically relevant conditions, biochemical methods developed to preserve the integrity of transient ribonucleoprotein assemblies, and mass spectrometry and cryo-electron microscopy to identify the composition and architecture of mRNPs. We will zoom-in on a set of paradigms in RNA biology that not only sample the breadth of mRNP diversity, but are also powerful model systems for linking structural information and biological function. We will investigate the molecular features in the three-dimensional organization of nuclear mRNPs from S. cerevisiae and of translationally repressed mRNPs in early developmental stages in D. melanogaster and X. laevis. For mRNPs undergoing active translation, we will investigate the transitions of human beta-globin mRNPs in the course of a surveillance process connected to disease. By studying these examples, we will glean fundamental insights into global principles governing the packaging of mRNPs and the remodeling of their three-dimensional features throughout a transcript’s life-cycle. The cumulative output will illuminate a central node of eukaryotic gene expression that is also particularly timely and relevant given recent developments in mRNA-based therapeutics.

With each newly detected exoplanet system, the planet formation theory is constantly gaining weight in the astrophysical research. The planets origin is a mystery which can only be solved by understanding the protoplanetary disks evolution. Recent disk observations by the new class of interferometer telescopes are challenging the existing theory of planet formation. They reveal astonishing detailed structures of spirals and rings in the dust emission which have never been seen before. Those structures are often claimed to be caused by embedded planets, which is difficult to explain with current models. This growing discrepancy between observation and theory forces us to realize: a novel disk modeling is essential to move on. Separate gas or dust evolution models have reached their limit and the gap between those has to be closed. With the UFOS project, I propose an unique and ambitious approach to unite gas and dust evolution models for protoplanetary disks. For the first time, a single global model will mutually link self-consistently: a) the transport of gaseous disk material, b) the radiative transfer, c) magnetic fields and their dissipation and d) the transport and growth of the solid material in form of dust grains. The development, performing and post-analysis of the models will initiate a new age for the planet formation research. The project results will achieve 1) unprecedented self-consistent precision to answer the question if those novel observed structures are caused by embedded planets or by the gas dynamics itself; 2) to find the locations of dust concentration and growth to unveil the birth places of planets and 3) to close the gap and finally unify self-consistent models of the disk evolution with the new class of observations. Only such advanced models combined with multi-wavelength observations, can show us the process of planet formation, and so explain the origin of the various of planets and exoplanets in our solar neighborhood and beyond.

Homochirality is one of the mysterious chemical benchmarks that is relevant to the origin of life. Biomacromolecules, constructed from the chiral building blocks, are mostly from exclusively either L- or D- structures, and the vast majority of the reactions in aqueous media are fine-tuned by chiral selectivity. However, although characterized by sum-frequency generation (SFG) spectroscopy and other techniques, whether and how the chiral biomolecules affect their hydration shells, through which intermolecular forces of such molecules are transmitted, are far from clear. Yet, the effect of perturbing the homochirality of biomacromolecules on their self-assembly is thus ambiguous. Here, I propose to use surface-anchored chiral short peptide molecules with a well-defined primary structure as a model. The structure and dynamics of the hydration shell of this peptide will be studied by chiral heterodyne detected sum-frequency (HD-SFG) spectroscopy, a nonlinear optical technique that provides information on hydration shells and their chirality. Using the solid phase peptide synthesis technique, chiral inversion will be induced at the level of a single monomer, blocks, and mixture of enantiomers. The self-assembly of peptide molecules will be characterized by atomic force microscopy for their morphology and SFG for their secondary structure. By quantitively comparing the spectrum of enantiomers, the dipole orientation of hydration water and their HB-network relaxation will be characterized using the O-H stretching band, which reflects thermodynamics and kinetics properties. Furthermore, the chiral inversion effect on self-assembly will be measured in the peptide’s amide I band, which reflects their packing. These results will shed light on chiral-induced water superstructure and self-assembly modulation, which is crucial for understanding the biological enrichment of homochirality and for anticancer/antiviral agent design.