Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes.

ABSTRACT: Misfolding and aggregation of prion protein (PrP) causes neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD) and scrapie. Besides the consensus that spontaneous conversion of normal cellular PrP^C into misfolded and aggregating PrP^Sc is the central event in prion disease, an alternative hypothesis suggests the generation of pathological PrP^Sc by rare translational frameshifting events in the octa-repeat domain of the PrP mRNA. Ribosomal frameshifting most commonly relies on a slippery site and an adjacent stable RNA structure to stall translating ribosome. Hence, it is crucial to unravel the secondary structure of the octa-repeat domain of PrP mRNA. Each of the five octa-repeats contains a motif (GGCGGUGGUGGCUGGG) which alone in vitro forms a G-q

SUBMITTER: Czech A 

PROVIDER: S-EPMC6384910 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature