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Updated: Apr 26, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

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Published on: August 8, 2017

Negative purifying selection drives prion and doppel protein evolution.

Kyriakos Tsangaras¹, Sergios-Orestis Kolokotronis, Rainer G Ulrich

¹Department of Wildlife Diseases, Leibniz Institute for Zoo and Wildlife Research, Alfred-Kowalke-Str. 17, 10315, Berlin, Germany.

Journal of Molecular Evolution

|July 21, 2014

Summary

Prion protein (PrP) and its paralog doppel protein (PRND) are under strong evolutionary selection. This study reveals relaxed selection in specific regions, offering insights into prion disease mechanisms and protein interactions.

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Protein Misfolding Cyclic Amplification of Prions

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Area of Science:

Neuroscience
Evolutionary Biology
Biochemistry

Background:

Misfolded prion protein (PrPSc) causes fatal transmissible spongiform encephalopathies.
Previous studies on evolutionary pressure on the prion gene (PRNP) yielded conflicting results.
Evolutionary mechanisms and interactions of prion paralogs like doppel (PRND) remain unexplored.

Purpose of the Study:

To investigate evolutionary selection pressures on the prion gene (PRNP) and doppel gene (PRND).
To identify coevolving sites between PRNP and PRND, suggesting protein interaction sites.
To clarify evolutionary mechanisms acting on prion and doppel proteins.

Main Methods:

Comparative genomic analysis of PRNP and PRND sequences.
Focus on taxonomic groups including primates, bovids, and rodents.
Analysis of selection pressure and identification of coevolving sites.

Main Results:

Both PRNP and PRND are under significant selective constraints.
Relaxed selection was observed on amino acid residues connecting alpha-helices 1 and 2 in both proteins.
Evidence suggests potential coevolutionary relationships between PRNP and PRND.

Conclusions:

Prion and doppel proteins are subject to strong evolutionary conservation.
Specific regions with relaxed selection may be critical for protein function or interaction.
Findings contribute to understanding the evolution of prion diseases and protein interactions.