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Nat Struct Mol Biol. 2011 Apr;18(4):443-50. doi: 10.1038/nsmb.2001. Epub 2011 Mar 13.

Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-β1.

Author information

1
Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology, Zürich, Switzerland.

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.

PMID:
21399644
DOI:
10.1038/nsmb.2001
[Indexed for MEDLINE]

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