Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14492
Title: Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-β1.
Authors: Cléry, A
Jayne, S
Benderska, N
Dominguez, C
Stamm, S
Allain, FH
First Published: Apr-2011
Citation: NAT STRUCT MOL BIOL, 2011, 18 (4), pp. 443-450
Abstract: Tra2-β1 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-β1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the β-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-β1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-β1 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-β1 and determined the functional sequence of Tra2-β1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.
DOI Link: 10.1038/nsmb.2001
eISSN: 1545-9985
Links: http://hdl.handle.net/2381/14492
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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