Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 7, Pages 853-U104Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1814
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Funding
- Roche Research Foundation for Biology
- Novartis Research Foundation
- Swiss National Science Foundation
- Structural Biology National Center of Competence in Research
- European Alternative Splicing Network
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The heterogeneous nuclear ribonucleoprotein (hnRNP) F is involved in the regulation of mRNA metabolism by specifically recognizing G-tract RNA sequences. We have determined the solution structures of the three quasi-RNA-recognition motifs (qRRMs) of hnRNP F in complex with G-tract RNA. These structures show that qRRMs bind RNA in a very unusual manner, with the G-tract 'encaged', making the qRRM a novel RNA binding domain. We defined a consensus signature sequence for qRRMs and identified other human qRRM-containing proteins that also specifically recognize G-tract RNAs. Our structures explain how qRRMs can sequester G-tracts, maintaining them in a single-stranded conformation. We also show that isolated qRRMs of hnRNP F are sufficient to regulate the alternative splicing of the Bcl-x pre-mRNA, suggesting that hnRNP F would act by remodeling RNA secondary and tertiary structures.
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