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Title: Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs
Authors: Dominguez, Cyril
Fisette, Jean-François
Chabot, Benoit
Allain, Frédéric H.-T.
First Published: 6-Jun-2010
Publisher: Nature Publishing Group
Citation: Nature Structural and Molecular Biology, 2010, 17 (7), pp. 853-862
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.
DOI Link: 10.1038/nsmb.1814
ISSN: 1545-9993
eISSN: 1545-9985
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2010, Nature Publishing Group. Deposited with reference to the publisher’s archiving policy available on the SHERPA/RoMEO website.
Appears in Collections:Published Articles, Dept. of Biochemistry

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