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• W2147219984 abstract "The [URE3] prion of Saccharomyces cerevisiae is a self-propagating inactive amyloid form of the Ure2 protein. Ure2p residues 1-65 constitute the prion domain, and the remaining C-terminal portion regulates nitrogen catabolism. We have examined the URE2 genes of wild-type isolates of S. cerevisiae and those of several pathogenic yeasts and a filamentous fungus. We find that the normal function of the S. cerevisiae Ure2p in nitrogen regulation is fully complemented by the Ure2p of Candida albicans, Candida glabrata, Candida kefyr, Candida maltosa, Saccharomyces bayanus, and Saccharomyces paradoxus, all of which have high homology in the C-terminal nitrogen regulation domain. However, there is considerable divergence of their N-terminal domains from that of Ure2p of S. cerevisiae. [URE3(Sc)] showed efficient transmission into S. cerevisiae ure2Delta cells if expressing a Ure2p of species within Saccharomyces. However, [URE3(Sc)] did not seed self-propagating inactivation of the Ure2p's from the other yeasts. When overexpressed as a fusion with green fluorescent protein, residues 5-47 of the S. cerevisiae prion domain are necessary for curing the [URE3] prion. Residues 11-39 are necessary for an inactivating interaction with the full-length Ure2p. A nearly identical region is highly conserved among many of the yeasts examined in this study, despite the wide divergence of sequences found in other parts of the N-terminal domains." @default.
• W2147219984 created "2016-06-24" @default.
• W2147219984 creator A5005390814 @default.
• W2147219984 creator A5068072238 @default.
• W2147219984 date "2002-12-10" @default.
• W2147219984 modified "2023-10-14" @default.
• W2147219984 title "Conservation of a portion of the <i>S. cerevisiae</i> Ure2p prion domain that interacts with the full-length protein" @default.
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• W2147219984 doi "https://doi.org/10.1073/pnas.162349599" @default.
• W2147219984 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/139898" @default.
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