The absence of a folded conformation of the RGG motifs is due to the abundance of hydrophilic and charged amino acids and to the lack of bulky hydrophobic groups that promote the formation of stable three-dimensional structures. The second most common class of intrinsically disordered regions in RBPs is represented by RGG-boxes (or GAR) that contain repeats of arginine and glycine residues. Indeed, recent reports revealed that intrinsically disordered regions (IDRs) are largely distributed in various RBPs sequences and contribute to RNA binding, cooperate with globular domains, and should play relevant roles in RNA interaction 6, 7, 8, 9. Some studies revealed that 3–11% of the human proteome is involved in RNA binding, but only a small fraction of proteins could be classified as typical globular RBPs 5. The capability of RBPs to bind RNA has been generally ascribed to the globular domains that possess a defined secondary structure, such as the RNA recognition motif (RRM), the K homology domain (KH), the zinc fingers (ZnF) and the DEAD box helicase motifs 1, 2, 3, 4. The “classic” RNA-binding proteins (RBPs) are a group of proteins playing central roles in the formation of ribonucleoprotein complexes as they participate in various gene expression processes. These interactions may play a role in the recognition of stem-loop RNA, without a disorder-to-order transition but retaining high dynamics. From a combination of EPR and NMR spectroscopies, we established that the two RGG regions transiently interact with the RRM itself. In this study, we present the characterization of a fragment of FUS comprising two RGG regions flanking the RNA Recognition Motif (RRM) alone and in the presence of a stem-loop RNA. The FET protein family, which includes FUS (Fused in Sarcoma), EWG (Ewing Sarcoma) and TAF15 (TATA binding association factor 15) proteins, is a group of RBPs containing three different long IDRs characterized by the presence of RGG motifs. Recent insights revealed that intrinsically disordered regions (IDRs) linking globular domains modulate their capability to interact with various sequences of RNA, but also regulate aggregation processes, stress-granules formation, and binding to other proteins. Our product lines include the research EPR product line ELEXSYS™, the compact EPR product lines EMXplus™ and EMXmicro™, the benchtop routine product line Magnettech ESR5000 and quality control product line microESR.Structural disorder represents a key feature in the mechanism of action of RNA-binding proteins (RBPs).
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