Proteins with RNA Chaperone Activity
(SFB project F1703 )
 

RNA molecules exhibit an astonishing flexibility, both structurally and functionally. This structural adaptability can lead to difficulties in defining a single native structure, known as the RNA folding problem. RNAs easily misfold and become trapped in inactive conformations that can be very stable and persistent. There are two types of proteins that are able to promote RNA folding: i) Specific RNA binding proteins that recognise distinct structural elements or sequences of a specific RNA, bind and stabilise their structure. ii) Proteins that do not bind specifically to a distinct RNA, but instead help RNAs to fold by resolving non-native conformations. This activity is termed “RNA chaperone activity”. This project aims at understanding the mode of action of proteins with RNA chaperone and RNA annealing activities. In this third funding period, we are studying several aspects of these proteins: we are comparing RNA helicases and RNA chaperones, especially concerning their energy requirement for unfolding RNA structures. We are performing mutational analysis on minimal protein domains to understand what a peptide must have to display RNA annealing or RNA chaperone activities with the goal to be able to design such peptides de novo. Using NMR, we want to understand dynamic changes both in RNAs and in proteins, which occur during their encounter.