Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that leads to a lack of voluntary muscle control. A similar disorder, frontotemporal dementia (FTD) presents as a progressive neuronal atrophy that leads to a loss of function in the temporal and frontal cortices. ALS and FTD share common inheritance pathways; however, the pathogenic mechanism by which the symptoms of these disorders develop is not well understood. One shared mutation leading to the development of ALS and FTD occurs in the fused in sarcoma/translocated in liposarcoma (<i>FUS/TLS</i>) gene, encoding for the protein FUS that plays an important role in regulating synaptic function and is purported to participate in specific transcriptional regulation. The FUS protein also contains an arginine-glycine-glycine (RGG) box, an RNA-binding domain that has been shown to specifically target and bind G-quadruplex secondary structures in messenger RNA (mRNA). We postulate that the MECP2 mRNA, shown to play a vital role in maintaining neuronal synapses, contains a G-quadruplex structure based on <i>in silico </i>analysis of the mRNA’s guanine-rich primary sequence. In this study we used different biophysical techniques to characterize this structure and its interactions with the RGG box domain of the FUS protein.

Biophysical analysis of a G-quadruplex structure in MECP2 messenger RNA

251st National Meeting (2016)

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