Poster abstracts
Poster number 53 submitted by Lydia Grimaldi
The interactions between hnRNP K mRNA and miR-1249-3P are mediated by a non-canonical G-quadruplex structure
Lydia Grimaldi (Duquesne University department of Chemistry and Biochemistry), Carlan Gray (Duquesne University department of Chemistry and Biochemistry), Bryan Kelleher (Duquesne University department of Chemistry and Biochemistry), Caylee Cunningham (Duquesne University department of Chemistry and Biochemistry), Mihaela-Rita Mihailescu (Duquesne University department of Chemistry and Biochemistry)
Abstract:
Amyotrophic lateral sclerosis (ALS), a neurodegenerative disease which results in progressive degeneration of motor neurons, has no cure. It has been shown that patients diagnosed with ALS have downregulated levels of a nucleic acid binding protein, hnRNP K, as well as of the microRNA (miR), miR-1249-3p. Previous work has shown that miR-1249-3p regulates the translation of hnRNP K. We have previously identified that a G quadruplex (GQ) structure forms in the 3’-untranslated (UTR) region of hnRNP K messenger RNA (mRNA) which encompasses the miR-1249-3p binding site. In this study we postulate that this GQ structure may mediate the interactions between the two RNAs. MiR binding electrophoretic mobility shift assays and fluorescence studies provided biophysical information about the stability of the hnRNP K mRNA GQ in different conditions and its ability to modulate the binding of the miR-1249-3p to bind to the hnRNP K mRNA.
References:
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Keywords: G Quadruplex , ALS