Nucleic Acids Research Advance Access originally published online on August 9, 2007
Nucleic Acids Research 2007 35(16):5379-5392; doi:10.1093/nar/gkm581
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Nucleic Acids Research, 2007, Vol. 35, No. 16 5379-5392
© 2007 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-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family
Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA
*To whom correspondence should be addressed. Tel: +1 412 396 1430; Fax: +1 412 396 5683; Email: mihailescum{at}duq.edu
Received January 17, 2007. Revised July 13, 2007. Accepted July 16, 2007.
Fragile X syndrome, the most common cause of inherited mental retardation, is caused by the transcriptional silencing of the fmr1 gene due to an unstable expansion of a CGG trinucleotide repeat and its subsequent hypermethylation in its 5' UTR. This gene encodes for the fragile X mental retardation protein (FMRP), an RNA-binding protein that has been shown to use its RGG box domain to bind to G quartet-forming RNA. In this study, we performed a detailed analysis of the interactions between the FMRP RGG box domain and one of its proposed RNA targets, human semaphorin 3F (S3F) RNA by using biophysical methods such as fluorescence, UV and circular dichroism spectroscopy. We show that this RNA forms a G quartet-containing structure, which is recognized with high affinity and specificity by the FMRP RGG box. In addition, we analyzed the interactions of human S3F RNA with the RGG box and RG cluster of the two FMRP autosomal paralogs, the FXR1P and FXR2P. We found that this RNA is bound with high affinity and specificity only by the FXR1P RGG box, but not by the FXR2P RG cluster. Both FMRP and FXR1P RGG box are able to unwind the G quartet structure of S3F RNA, however, the peptide concentrations required in this process are very different: a ratio of 1:6 RNA:FMRP RGG box versus 1:2 RNA:FXR1P RGG box.
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