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Updated: Apr 18, 2026

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

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

Published on: August 8, 2017

What makes a protein sequence a prion?

Raimon Sabate¹, Frederic Rousseau², Joost Schymkowitz²

¹Departament de Fisicoquímica, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain; Institut de Nanociència i Nanotecnologia (IN2UB), Universitat de Barcelona, Barcelona, Spain.

Plos Computational Biology

|January 9, 2015

Summary

This summary is machine-generated.

Amyloid diseases like Alzheimer's can spread between cells via a prion-like mechanism. Specific short sequences within glutamine/asparagine-rich regions, not just composition, drive this prion behavior.

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Published on: January 8, 2015

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Amyloid diseases, including Alzheimer's and Parkinson's, were traditionally viewed as arising from de novo aggregation within cells.
Recent research indicates a prion-like mechanism where amyloids can propagate between cells, cross-seeding aggregation.
Understanding the primary sequence determinants of this prion transmissibility remains a significant challenge.

Purpose of the Study:

To investigate how the primary amino acid sequence encodes prion behavior in amyloid formation.
To challenge the prevailing hypothesis that amino acid composition of glutamine/asparagine-rich regions solely dictates prionogenicity.
To identify specific sequence features responsible for the prion properties of amyloids.

Main Methods:

Analysis of intrinsically disordered glutamine/asparagine (Q/N)-rich regions in protein sequences.
Evaluation of the role of specific short amyloid-prone sequences versus overall amino acid composition.
Investigating the influence of structural and compositional context on prion behavior.

Main Results:

Prion behavior is determined by the presence and potency of specific short amyloid-prone sequences within Q/N-rich regions.
Amino acid composition alone is insufficient to explain prionogenicity.
The structural and compositional context modulates the prion activity of these sequences.

Conclusions:

Prion-like propagation of amyloids is encoded by specific short sequence motifs, not just regional composition.
This finding offers a refined understanding of amyloid disease mechanisms and prion transmissibility.
Provides a framework for identifying and evaluating potential prion candidate sequences in proteomes.