BPS2026 – Mechanisms of co-translational folding and assembly of proteins

Many critical steps of enzymatic processing, membrane targeting, native folding and assembly of newly synthesized proteins occur co-translationally, implying that protein maturation and decoding of genetic information by the ribosome are coupled processes. Our research aims to dissect the flux of the nascent chain proteome through the network of co-translationally engaged chaperones and quality control machinery, using ribosome profiling, biochemical approaches, and cryo-EM. Here, we will report insights into the working principles of ribosome-associated as well as downstream-acting chaperones in protein folding and address how the co-translationally assembly of protein complexes is achieved and coordinated with the progression of translation.