{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bonucci A"],"funding":["H2020 Research Infrastructures","Ministero dell’Istruzione, dell’Università e della Ricerca","Regione Toscana"],"pagination":["20956"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7708983"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Structural disorder represents a key feature in the mechanism of action of RNA-binding proteins (RBPs). 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. 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. 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. From a combination of EPR and NMR spectroscopies, we established that the two RGG regions transiently interact with the RRM itself. These interactions may play a role in the recognition of stem-loop RNA, without a disorder-to-order transition but retaining high dynamics."],"journal":["Scientific reports"],"pubmed_title":["A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS."],"pmcid":["PMC7708983"],"funding_grant_id":["731005","POR-FSE 2014-2020","FOE"],"pubmed_authors":["Pierattelli R","Murrali MG","Bonucci A","Banci L"],"additional_accession":[]},"is_claimable":false,"name":"A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS.","description":"Structural disorder represents a key feature in the mechanism of action of RNA-binding proteins (RBPs). 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. 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. 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. From a combination of EPR and NMR spectroscopies, we established that the two RGG regions transiently interact with the RRM itself. These interactions may play a role in the recognition of stem-loop RNA, without a disorder-to-order transition but retaining high dynamics.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2024-11-19T15:48:48.437Z","creation":"2021-02-20T03:03:47Z"},"accession":"S-EPMC7708983","cross_references":{"pubmed":["33262375"],"doi":["10.1038/s41598-020-77899-x"]}}