| Autor: |
Bonucci A; CERM - Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy.; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy., Murrali MG; CERM - Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy., Banci L; CERM - Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it., Pierattelli R; CERM - Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy. roberta.pierattelli@unifi.it.; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. roberta.pierattelli@unifi.it. |
| Abstrakt: |
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. |
