The [URE3] prion is not conserved among Saccharomyces species.
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.
Talarek
Nicolas
N
IBGC-CNRS/Université Victor Segalen Bordeaux2, UMR 5095, 33077 Bordeaux, France. nicolas_talarek@dfci.harvard.edu
Maillet
Laurent
L
Cullin
Christophe
C
Aigle
Michel
M
D000595:Amino Acid Sequence; D017124:Conserved Sequence / Q000235:genetics*; D019143:Evolution, Molecular; D005816:Genetic Complementation Test; D005979:Glutathione Peroxidase; D008969:Molecular Sequence Data; D010802:Phylogeny; D011328:Prions / Q000235:genetics* / Q000378:metabolism; D012440:Saccharomyces / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae