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Nucleic Acids Research 2006 34(13):3634-3645; doi:10.1093/nar/gkl488
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Published online 2 August 2006

Nucleic Acids Research, 2006, Vol. 34, No. 13 3634-3645
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.

Article

NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition

Cyril Dominguez and Frédéric H.-T. Allain*

Institute of Molecular Biology and Biophysics, ETH Zürich CH-8093 Zürich, Switzerland

*To whom correspondence should be addressed: Tel: +41 1 633 3940; Fax: +41 1 633 1294; Email: allain{at}mol.biol.ethz.ch

Received May 23, 2006. Revised June 28, 2006. Accepted June 28, 2006.

The heterogeneous nuclear ribonucleoprotein (hnRNP) F belongs to the hnRNP H family involved in the regulation of alternative splicing and polyadenylation and specifically recognizes poly(G) sequences (G-tracts). In particular, hnRNP F binds a G-tract of the Bcl-x RNA and regulates its alternative splicing, leading to two isoforms, Bcl-xS and Bcl-xL, with antagonist functions. In order to gain insight into G-tract recognition by hnRNP H members, we initiated an NMR study of human hnRNP F. We present the solution structure of the three quasi RNA recognition motifs (qRRMs) of hnRNP F and identify the residues that are important for the interaction with the Bcl-x RNA by NMR chemical shift perturbation and mutagenesis experiments. The three qRRMs exhibit the canonical ß{alpha}ßß{alpha}ß RRM fold but additional secondary structure elements are present in the two N-terminal qRRMs of hnRNP F. We show that qRRM1 and qRRM2 but not qRRM3 are responsible for G-tract recognition and that the residues of qRRM1 and qRRM2 involved in G-tract interaction are not on the ß-sheet surface as observed for the classical RRM but are part of a short ß-hairpin and two adjacent loops. These regions define a novel interaction surface for RNA recognition by RRMs.


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