Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA)
octo-repeat PrP mRNA mutant (RNA), PrPmRNA_mut, human PrP ORF
Biological species
human PrP ORF
Citation
Journal: Sci Rep / Year: 2019 Title: Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Authors: Andreas Czech / Petr V Konarev / Ingrid Goebel / Dmitri I Svergun / Peter R Wills / Zoya Ignatova / 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 ...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.
Contact author
Petr Konarev (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)
Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm
Detector
Name: Pilatus 2M
Scan
Title: Mutant mammalian prion protein mRNA (octo-repear PrP mRNA mutant) Measurement date: Jun 6, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
Min
Max
Q
0.1069
3.7878
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 442 /
Min
Max
Q
0.11
3.786
P(R) point
1
442
R
0
24
Result
Type of curve: merged
Experimental
Standard
Standard error
Porod
MW
130 kDa
130 kDa
20
125 kDa
Volume
-
-
-
150 nm3
P(R)
P(R) error
Guinier
Guinier error
Forward scattering, I0
25410
2100
25456
2100
Radius of gyration, Rg
6.96 nm
0.07
6.97 nm
0.07
Min
Max
Error
D
-
24
0.8
Guinier point
1
20
-
+
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