PrionW: A server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores

Rafael Zambrano, Oscar Conchillo-Sole, Valentin Iglesias, Ricard Illa, Frederic Rousseau, Joost Schymkowitz, Raimon Sabate, Xavier Daura, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)

Abstract

© The Author(s) 2015. Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. Prionlike conversion underlies important biological processes but is also connected to human disease. Yeast prions are the best understood transmissible amyloids. In these proteins, prion formation from an initially soluble state involves a structural conversion, driven, in many cases, by specific domains enriched in glutamine/asparagine (Q/N) residues. Importantly, domains sharing this compositional bias are also present in the proteomes of higher organisms, thus suggesting that prion-like conversion might be an evolutionary conserved mechanism. We have recently shown that the identification and evaluation of the potency of amyloid nucleating sequences in putative prion domains allows discrimination of genuine prions. PrionW is a web application that exploits this principle to scan sequences in order to identify proteins containing Q/N enriched prion-like domains (PrLDs) in large datasets. When used to scan the complete yeast proteome, PrionW identifies previously experimentally validated prions with high accuracy. Users can analyze up to 10 000 sequences at a time, PrLD-containing proteins are identified and their putative PrLDs and amyloid nucleating cores visualized and scored. The output files can be downloaded for further analysis. PrionW server can be accessed at http://bioinf.uab.cat/prionw/.
Original languageEnglish
Pages (from-to)W331-W337
JournalNucleic Acids Research
Volume43
Issue numberW1
DOIs
Publication statusPublished - 14 May 2015

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