New insights into the auxiliary domains of eukaryotic RNA binding proteins.
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.
Biamonti
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Istituto di Genetica Biochimica ed Evoluzionistica del CNR, Pavia, Italy.
Riva
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D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D016601:RNA-Binding Proteins; D012313:RNA