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|Title:||Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs|
Allain, Frédéric H.-T.
|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.|
|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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|2010-NSMB.pdf||Post-review (final submitted)||7.36 MB||Adobe PDF||View/Open|
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