期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 18, 期 4, 页码 443-U78出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2001
关键词
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资金
- SNF-NCCR Structural Biology
- Muscular Dystrophy Association
- European Molecular Biology Organization
- EURASNET
Tra2-beta 1 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-beta 1 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-beta 1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-beta 1 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-beta 1 and determined the functional sequence of Tra2-beta 1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.
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