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

Andreas Czech1, Petr V Konarev2,3, Ingrid Goebel4

  • 1Institute of Biochemistry and Molecular Biology University of Hamburg, Hamburg, Germany. andreas.czech@chemie.uni-hamburg.de.

Scientific Reports
|February 23, 2019
PubMed

Insights

Prion protein mRNA

Area of Science:

  • Neurodegenerative diseases
  • Molecular biology
  • Prion protein structure

Background:

  • Prion protein (PrP) misfolding causes neurodegenerative diseases like CJD.
  • An alternative hypothesis suggests pathological PrP generation via mRNA translational frameshifting.
  • Understanding PrP mRNA secondary structure is key to investigating this hypothesis.

Purpose of the Study:

  • To determine the secondary structure of the full-length prion protein (PrP) octa-repeat mRNA region.
  • To investigate the potential for G-quadruplex formation within this domain.

Main Methods:

  • Dynamic Light Scattering (DLS)
  • Small Angle X-ray Scattering (SAXS)
  • Circular Dichroism (CD) spectroscopy
  • Selective 2'-hydroxyl acylation analysis by primer extension (SHAPE)

Main Results:

  • The PrP octa-repeat mRNA forms stable A-helical hairpins.
  • No evidence of G-quadruplex structure was detected.
  • This was observed even when using G-quadruplex stabilizing agents.

Conclusions:

  • The PrP octa-repeat mRNA region does not form G-quadruplex structures.
  • Findings suggest A-helical hairpins are the predominant secondary structure.
  • This provides critical insights into the mRNA's role in potential prion disease mechanisms.

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