Abstract
Fragile X Syndrome (FXS) is the most common form of inherited mental retardation affecting approximately 1 in 4,000 males and 1 in 8,000 females. FXS is linked to the expansion of cytosine-guanine-guanine trinucleotide repeats in the fragile X mental retardation 1 (fmr1) gene. This expansion causes hypermethylation of the cytosines, transcriptional silencing of fmr1, and loss of the fragile X mental retardation protein (FMRP). Normally, FMRP regulates the translation of a class of mRNAs, which adopt the G quadruplex structure, at neuronal dendrites. One mechanism by which the protein might perform its translation regulator function is the reversible phosphorylation of FMRP. In human FMRP, the highly conserved Serine 500 is the major phosphorylation site. This site is directly N-terminal of the FMRP arginine-glycine-glycine box, which specifically binds to the mRNA G quadruplex structure. In this study, we utilized different biochemical and biophysical methods to analyze the translation regulator function of both phosphorylated and unphosphorylated FMRP on the G quadruplex forming Microtubule Associated Protein 1B mRNA.
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