The [URE3] Prion Is Not Conserved Among Saccharomyces Species

Talarek, Nicolas; Maillet, Laurent; Cullin, Christophe; Aigle, Michel

doi:10.1534/genetics.105.043489

Cited by 38 publications

(41 citation statements)

References 72 publications

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“…As reported by Talarek et al (2005), we found that we could not select [URE3para] para in S. paradoxus strain MA578, even on overproduction of Ure2p para . We tested whether the [URE3para] para , generated in S. cerevisiae carrying the paradoxus URE2 gene in place of that of cerevisiae, could be transmitted to S. paradoxus by cytoduction (cytoplasmic mixing) to strain MA578, and found that none of several [URE3para] variants were transmitted (Table 2 and data not shown).…”

Section: Nomenclaturesupporting

confidence: 61%

“…Because of the difficulties of Candida genetics, we chose to examine the prion-forming abilities of C. albicans and C. glabrata Ure2p in S. cerevisiae, an approach often used by others as well (Chernoff et al 2000;Kushnirov et al 2000;Santoso et al 2000;Nakayashiki et al 2001). However, while the Ure2p of S. paradoxus forms a prion in S. cerevisiae (Edskes and Wickner 2002;Edskes et al 2009), it was found to not form [URE3] in S. paradoxus itself (Talarek et al 2005), casting doubt on this approach.…”

Section: Methodsmentioning

confidence: 99%

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Prion-Forming Ability of Ure2 of Yeasts Is Not Evolutionarily Conserved

et al. 2011

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ABSTRACT[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We show that wild S. paradoxus can be infected with a [URE3] prion, supporting the use of S. cerevisiae as a prion test bed. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion in S. cerevisiae, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3] as judged by its performance in S. cerevisiae. These results suggest that the sequence is not conserved to preserve prion forming ability.

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Section: Nomenclaturesupporting

confidence: 61%

Section: Methodsmentioning

confidence: 99%

Prion-Forming Ability of Ure2 of Yeasts Is Not Evolutionarily Conserved

et al. 2011

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“…Deletion of the URE2 gene is nonlethal, implying that, at least in the lab environment, both enzymatic and regulatory functions are dispensable. It remains uncertain whether the [URE3] prion ever crops up in the wild [66] and the ability of Ure2 protein homologues to switch to the [URE3] prion form is conserved in some yeast species but not others [67,68]. There nevertheless remains the possibility that the additional epigenetic variability provided by the prionswitch provides an advantage in surviving changes in environment.…”

Section: Relationship Between Enzymatic Regulatory and Prion Functiomentioning

confidence: 99%

“…The loss of the nitrogen regulatory function of Ure2 in strains containing the [URE3] prion, while GPx activity is maintained, is probably due to the relative sizes of the ligands involved in these reactions, and not any reflection of the relative importance of the respective activities. The purpose and evolutionary implications of fungal prions are discussed elsewhere [8,9,66,67,68].…”

Section: Relationship Between Enzymatic Regulatory and Prion Functiomentioning

confidence: 99%

The yeast prion protein Ure2: Structure, function and folding

Lian

Jiang

Zhang

et al. 2006

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The Saccharomyces cerevisiae protein Ure2 functions as a regulator of nitrogen metabolism and as a glutathione-dependent peroxidase. Ure2 also has the characteristics of a prion, in that it can undergo a heritable conformational change to an aggregated state; the prion form of Ure2 loses the regulatory function, but the enzymatic function appears to be maintained. A number of factors are found to affect the prion properties of Ure2, including mutation and expression levels of molecular chaperones, and the effect of these factors on structure and stability are being investigated. The relationship between structure, function and folding for the yeast prion Ure2 are discussed.

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“…Homologs of prion protein Ure2 from the closely related Saccharomyces species exhibited no species barrier, although researchers disagreed on whether Saccharomyces paradoxus Ure2 is capable of forming a prion at all (22)(23)(24). Therefore, it remained unclear whether prion species barrier exists in yeast at the levels of sequence divergence that are comparable to those observed in mammals.…”

mentioning

confidence: 99%

Prion species barrier between the closely related yeast proteins is detected despite coaggregation

Chen

Newnam²,

Chernoff³

2007

Proc. Natl. Acad. Sci. U.S.A.

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Prions are self-perpetuating and, in most cases, aggregation-prone protein isoforms that transmit neurodegenerative diseases in mammals and control heritable traits in yeast. Prion conversion requires a very high level of identity of the interacting protein sequences. Decreased transmission of the prion state between divergent proteins is termed ''species barrier'' and was thought to occur because of the inability of divergent prion proteins to coaggregate. Species barrier can be overcome in cross-species infections, e.g., from ''mad cows'' to humans. We studied the counterparts of yeast prion protein Sup35, originated from three different species of the Saccharomyces sensu stricto group and exhibiting the range of prion domain divergence that overlaps with the range of divergence observed among distant mammalian species. All three proteins were capable of forming a prion in Saccharomyces cerevisiae, although prions formed by heterologous proteins were usually less stable than the endogenous S. cerevisiae prion. Heterologous Sup35 proteins coaggregated in the S. cerevisiae cells. However, in vivo cross-species prion conversion was decreased and in vitro polymerization was cross-inhibited in at least some heterologous combinations, thus demonstrating the existence of prion species barrier. Moreover, the barrier between the S. cerevisiae protein and its Saccharomyces paradoxus and Saccharomyces bayanus counterparts was asymmetric both in vivo and in vitro. Our data show that a decreased cross-species prion transmission does not necessarily correlate with a lack of crossspecies coaggregation, suggesting that species-specificity of prion transmission is controlled at the level of conformational transition rather than coaggregation.amyloid ͉ Saccharomyces bayanus ͉ Saccharomyces cerevisiae ͉ Saccharomyces paradoxus ͉ Sup35

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The [URE3] Prion Is Not Conserved Among Saccharomyces Species

Cited by 38 publications

References 72 publications

Prion-Forming Ability of Ure2 of Yeasts Is Not Evolutionarily Conserved

Prion-Forming Ability of Ure2 of Yeasts Is Not Evolutionarily Conserved

The yeast prion protein Ure2: Structure, function and folding

Prion species barrier between the closely related yeast proteins is detected despite coaggregation

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