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TitleOcta-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes.
Journal, issue, pagesSci Rep, Vol. 9, Issue 1, Page 2465, Year 2019
Publish dateFeb 21, 2019
AuthorsAndreas Czech / Petr V Konarev / Ingrid Goebel / Dmitri I Svergun / Peter R Wills / Zoya Ignatova /
PubMed AbstractMisfolding and aggregation of prion protein (PrP) causes neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD) and scrapie. Besides the consensus that spontaneous conversion of normal ...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 into misfolded and aggregating PrP is the central event in prion disease, an alternative hypothesis suggests the generation of pathological PrP 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-quadruplex. Since the propensity of mRNA to form secondary structure depends on the sequence context, we set to determine the structure of the complete octa-repeat region. We assessed the structure of full-length octa-repeat domain of PrP mRNA using dynamic light scattering (DLS), small angle X-ray scattering (SAXS), circular dichroism (CD) spectroscopy and selective 2'-hydroxyl acylation analysis by primer extension (SHAPE). Our data show that the PrP octa-repeat mRNA forms stable A-helical hairpins with no evidence of G-quadruplex structure even in the presence of G-quadruplex stabilizing agents.
External linksSci Rep / PubMed:30792490 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDDG5:
Mammalian prion protein mRNA (PrP mRNA wild type) (octo-repeat PrP mRNA, PrPmRNA)
Method: SAXS/SANS

SASDDH5:
Mammalian prion protein mRNA (PrP mRNA wild type) with KCl
Method: SAXS/SANS

SASDDJ5:
Mammalian prion protein mRNA (PrP mRNA wild type) with LiCl
Method: SAXS/SANS

SASDDK5:
Mammalian prion protein mRNA (PrP mRNA wild type) with KCl and pyridostatin (PDS)
Method: SAXS/SANS

SASDDL5:
Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA)
Method: SAXS/SANS

SASDDM5:
Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA) with KCl
Method: SAXS/SANS

SASDDN5:
Mutant mammalian prion protein mRNA (octo-repear PrP mRNA) with LiCl
Method: SAXS/SANS

SASDDP5:
Mutant mammalian prion protein mRNA (octo-repear PrP mRNA) with KCl and pyridostatin (PDS)
Method: SAXS/SANS

Source
  • Human prp orf

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