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Issue 12, 2008
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Fragile X mental retardation protein recognition of G quadruplex structure per se is sufficient for high affinity binding to RNA

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Abstract

Fragile X syndrome, the most common form of inherited mental retardation is caused by the expansion of a CGG trinucleotide repeat in the fragile X mental retardation 1 (fmr1) gene. The abnormal expansion of the CGG repeat causes hypermethylation and subsequent silencing of the fmr1gene, resulting in the loss of the fragile X mental retardation protein (FMRP). FMRP has been shown to use its arginine-glycine-glycine rich region (RGG box) to bind to messenger RNAs that form G quadruplex structures. Several studies reported that the G quadruplex RNA recognition alone is not sufficient for FMRP RGG box binding and that an additional stem and/or a G quadruplex–stem junction region may also be important in recognition. In this study we have used biophysical methods such as fluorescence, UV, CD and NMR spectroscopy to demonstrate that the recognition of the RNA G quadruplex structure per se, in the absence of a stem region, is sufficient for the FMRP high affinity and specific binding. These findings indicate that the presence of a stem structure in some of the FMRP G quadruplex forming mRNAs is not a requirement for protein recognition as previously believed, but rather for the proper formation of the correct RNA G quadruplex structure recognized by FMRP.

Graphical abstract: Fragile X mental retardation protein recognition of G quadruplex structure per se is sufficient for high affinity binding to RNA

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Publication details

The article was received on 22 Jul 2008, accepted on 03 Sep 2008 and first published on 27 Oct 2008


Article type: Paper
DOI: 10.1039/B812537F
Citation: Mol. BioSyst., 2008,4, 1212-1219
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    Fragile X mental retardation protein recognition of G quadruplex structure per se is sufficient for high affinity binding to RNA

    M. Bole, L. Menon and M. Mihailescu, Mol. BioSyst., 2008, 4, 1212
    DOI: 10.1039/B812537F

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