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Tra2-beta1 is a unique splicing factor as its single RNA recognition motif (RRM) is located between two RS (arginine-serine) domains. To understand how this protein recognizes its RNA target, we solved the structure of Tra2-beta1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the beta-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-beta1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-beta1 and RNA mutations on the splicing of SMN2 exon 7, we validated the importance of the RNA-protein contacts observed in the structure for the function of Tra2-beta1 and determined the functional sequence of Tra2-beta1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.
Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1.,Clery A, Jayne S, Benderska N, Dominguez C, Stamm S, Allain FH Nat Struct Mol Biol. 2011 Apr;18(4):443-50. Epub 2011 Mar 13. PMID:21399644[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Clery A, Jayne S, Benderska N, Dominguez C, Stamm S, Allain FH. Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1. Nat Struct Mol Biol. 2011 Apr;18(4):443-50. Epub 2011 Mar 13. PMID:21399644 doi:10.1038/nsmb.2001
