The [URE3] prion is not conserved among Saccharomyces species

• Published in: Genetics (Austin) 2005-09, Vol.171 (1), p.23-34
• Main Authors: Talarek, Nicolas, Maillet, Laurent, Cullin, Christophe, Aigle, Michel
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Biochemistry, Molecular Biology; Conserved Sequence - genetics; Evolution, Molecular; Evolutionary biology; Genetic Complementation Test; Genetics; Glutathione Peroxidase; Investigations; Life Sciences; Molecular biology; Molecular Sequence Data; Phylogeny; Prions; Prions - genetics; Prions - metabolism; Proteins; Saccharomyces; Saccharomyces - genetics; Saccharomyces - growth & development; Saccharomyces - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - growth & development; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces paradoxus; Saccharomyces uvarum; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Yeast
• ISSN: 0016-6731; 1943-2631; 1943-2631
• DOI: 10.1534/genetics.105.043489

The [URE3] prion of Saccharomyces cerevisiae is a self-propagating inactive form of the nitrogen catabolism regulator Ure2p. To determine whether the [URE3] prion is conserved in S. cerevisiae-related yeast species, we have developed genetic tools allowing the detection of [URE3] in Saccharomyces paradoxus and Saccharomyces uvarum. We found that [URE3] is conserved in S. uvarum. In contrast, [URE3] was not detected in S. paradoxus. The inability of S. paradoxus Ure2p to switch to a prion isoform results from the primary sequence of the protein and not from the lack of cellular cofactors as heterologous Ure2p can propagate [URE3] in this species. Our data therefore demonstrate that [URE3] is conserved only in a subset of Saccharomyces species. Implications of our finding on the physiological and evolutionary meaning of the yeast [URE3] prion are discussed.