New insights into the auxiliary domains of eukaryotic RNA binding proteins

Abstract

Eukaryotic RNA binding proteins (RBP) are key players in RNA processing and in post-transcriptional regulation of gene expression. By interacting with RNA and other factors and by modulating the RNA structure, they promote the assembly of a great variety of specific ribonucleoprotein complexes. Many RBPs are composed of highly structured and conserved RNA binding domains (RBD) linked to unstructured and divergent auxiliary domains; such modular structure can account for a multiplicity of interactions. In this context, the auxiliary domains emerge as essential partners of the RBDs in both RNA binding and functional specialisation. Moreover, the determinants of biologically important functions, such as strand annealing, protein-protein interactions, nuclear localization and activity in in vitro splicing, seem to reside in the auxiliary domains. The structural and functional properties of these domains suggest their possible derivation from ancestral non-specific RNA binding polypeptides.