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Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs

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journal contribution
posted on 24.10.2012, 08:58 by Cyril Dominguez, Jean-François Fisette, Benoit Chabot, Frédéric H.-T. Allain
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.

History

Citation

Nature Structural and Molecular Biology, 2010, 17 (7), pp. 853-862

Version

AM (Accepted Manuscript)

Published in

Nature Structural and Molecular Biology

Publisher

Nature Publishing Group

issn

1545-9993

eissn

1545-9985

Copyright date

2010

Available date

24/10/2012

Publisher version

http://www.nature.com/nsmb/journal/v17/n7/full/nsmb.1814.html

Language

eng