Premium
The yeast prion [ URE3 ] can be greatly induced by a functional mutated URE2 allele
Author(s) -
FernandezBellot Eric,
Guillemet Elisabeth,
Cullin Christophe
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.13.3215
Subject(s) - cullin , biology , humanities , library science , genetics , philosophy , gene , computer science , ubiquitin ligase , ubiquitin
The non‐Mendelian element [ URE3 ] of yeast is considered to be a prion form of the Ure2 protein. The [ URE3 ] phenotype occurs at a frequency of 10 −5 in haploid yeast strains, is reversible, and its frequency is increased by overexpressing the URE2 gene. We created a new mutant of the Ure2 protein, called H2p, which results in a 1000‐fold increase in the rate of [ URE3 ] occurrence. To date, only the overexpression of various C‐terminal truncated mutants of Ure2p gives rise to a comparable level. The h2 allele is, thus, the first characterized URE2 allele that induces prion formation when expressed at a low level. By shuffling mutated and wild‐type domains of URE2 , we also created the first mutant Ure2 protein that is functional and induces prion formation. We demonstrate that the domains of URE2 function synergistically in cis to induce [ URE3 ] formation, which highlights the importance of intramolecular interactions in Ure2p folding. Additionally, we show using a green fluorescent protein (GFP) fusion protein that the h2 allele exhibits numerous filiform structures that are not generated by the wild‐type protein.