Certain guanine-rich segments of RNA have recently been shown to fold into the G quadruplex structure.  Four guanine residues form a planar conformation (G quartet) stabilized by Hoogsteen base pairing.  Sets of these planar G quartets stack to form the G quadruplex structure, stabilized by a central core of potassium ions between each plane.  It has been proposed that the presence of G quadruplexes in the 5'-UTR, coding region, and 3'-UTR of mRNAs regulates various processes of the respective mRNA.  In particular, it has been demonstrated that the presence of a G quadruplex in the mRNA 5'-UTR acts a translation regulation element.  Additionally, bioinformatics analyses have revealed that 2334 sequences predicted to fold into the G quadruplex structure reside in the 5'-UTRs of human mRNA transcripts from known protein coding genes.  Despite the emerging evidence supporting the G quadruplex structure located in the mRNA 5'-UTR as a regulatory mechanism, correlations between structural properties, thermodynamic characteristics, and translation regulation activity remain unclear.  In this study, biophysical and biochemical methods such as UV, CD, and NMR spectroscopy were employed to characterize 18-21mer segments located in the 5'UTR of human mRNAs, particularly those encoding neuronal proteins and proteins potentially associated with disease.  These findings have demonstrated that every target sequence successfully formed a G quadruplex structure, and there exists high similarity regarding structural and thermodynamic properties between the various G quadruplexes.  These results illustrate consistencies that contribute to the overall understanding of translation regulation via the G quadruplex structure and provide insight into potential targets for disease treatment and prevention

Consistent thermodynamic and structural properties of G quadruplex structures from the 5'-UTR of human mRNAs

247th National Meeting (2014)

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