Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.
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Dominguez C, Fisette JF, Chabot B, Allain FH
Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.
Nat Struct Mol Biol. 2010 Jul;17(7):853-61. doi: 10.1038/nsmb.1814. Epub 2010 Jun 6.
- PubMed ID
- 20526337 [ View in PubMed]
- Abstract
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.