Proteins and ribonucleic acids associate to a large number of macromolecular complexes (RNPs) in living cells. Many of them are acting together as crucial players in numerous biological networks. Consequently, impaired RNP formation and function are linked to cellular malfunction and severe disease. Accordingly, analyses of dynamic RNP-assembly processes and the regulation of RNP function became central topics in recent research.
Formation and function of RNPs depend on the interplay of many RNA-producing or RNA-containing protein complexes. First, the regulated synthesis of the RNA moiety is crucial for RNP formation and has a major impact in the coordination of co-transcriptional and post-transcriptional RNA-modifications. Second, a functional network of many RNA-binding, RNA-modifying and RNA-folding complexes participates to maturate nascent RNPs. Third, the interplay of different RNPs is crucial for RNP activity, as exemplified by the regulation of ribosome activity by microRNA-containing protein complexes (miRNPs).
Among RNPs, ribosomes, the cellular factories for protein production, are the among the most intricate and complex RNP-assemblies in the cell. Their biogenesis is tightly regulated and requires the coordinated activity of many cellular processes and can therefore be considered as a well-suited model system to study mechanisms of RNP biogenesis. Ribosomes form the center of our investigations. We propose to analyze the many overlapping processes leading to mature ribosomes, compare them with the formation of other RNPs and focus on their interaction with RNAs or other RNPs which are important to control their activity. In summary, our combined efforts will allow us to understand common principles and specific features of RNP formation. We will further get insight into the complex interplay between different RNPs to regulate important cellular processes.