MB&B Seminar: "Mechanisms of Co-translational Folding and Assembly of Newly Synthesized Proteins"

We are using ribosome profiling technology to dissect the flux of the nascent chain proteome through the system of co-translationally engaged chaperones. This allowed us to reveal principles of functional networking of the co-translational chaperone machineries that promote the formation of correctly folded proteins. we also show that the assembly of oligomers frequently occurs co-translationally, involving the engagement of nascent subunits.