Title: What makes a protein sequence a prion?
Authors: Sabate, Raimon
Rousseau, Frederic
Schymkowitz, Joost
Ventura, Salvador # ×
Issue Date: Jan-2015
Publisher: Public Library of Science
Series Title: PLoS Computational Biology vol:11 issue:1 pages:e1004013
Article number: 10.1371/journal.pcbi.1004013
Abstract: Typical amyloid diseases such as Alzheimer's and Parkinson's were thought to exclusively result from de novo aggregation, but recently it was shown that amyloids formed in one cell can cross-seed aggregation in other cells, following a prion-like mechanism. Despite the large experimental effort devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the primary sequence. In many cases, prion structural conversion is driven by the presence of relatively large glutamine/asparagine (Q/N) enriched segments. Several studies suggest that it is the amino acid composition of these regions rather than their specific sequence that accounts for their priogenicity. However, our analysis indicates that it is instead the presence and potency of specific short amyloid-prone sequences that occur within intrinsically disordered Q/N-rich regions that determine their prion behaviour, modulated by the structural and compositional context. This provides a basis for the accurate identification and evaluation of prion candidate sequences in proteomes in the context of a unified framework for amyloid formation and prion propagation.
ISSN: 1553-734X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Switch Laboratory
× corresponding author
# (joint) last author

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