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Vol. 14, Issue 8, 3449-3458, August 2003
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¶
IBGC, 33077 Bordeaux cedex, France;
* CGM, 91190 Gif-sur-Yvette Cedex, France;
Department of Biosciences, University of Kent at Canterbury, Canterbury, Kent
CT2 7NJ, United Kingdom; and
IJM, 75251 Paris cedex 05, France
Submitted January 15, 2003;
Revised April 4, 2003;
Accepted April 4, 2003
Monitoring Editor: Peter Walter
The yeast inheritable [URE3] element corresponds to a prion form of the nitrogen catabolism regulator Ure2p. We have isolated several orthologous URE2 genes in different yeast species: Saccharomyces paradoxus, S. uvarum, Kluyveromyces lactis, Candida albicans, and Schizosaccharomyces pombe. We show here by in silico analysis that the GST-like functional domain and the prion domain of the Ure2 proteins have diverged separately, the functional domain being more conserved through the evolution. The more extreme situation is found in the two S. pombe genes, in which the prion domain is absent. The functional analysis demonstrates that all the homologous genes except for the two S. pombe genes are able to complement the URE2 gene deletion in a S. cerevisiae strain. We show that in the two most closely related yeast species to S. cerevisiae, i.e., S. paradoxus and S. uvarum, the prion domains of the proteins have retained the capability to induce [URE3] in a S. cerevisiae strain. However, only the S. uvarum full-length Ure2p is able to behave as a prion. We also show that the prion inactivation mechanisms can be cross-transmitted between the S. cerevisiae and S. uvarum prions.
Abbreviations used: USA, ureidosuccinate; Gal, galactose; Glu, glucose; Sc, Sacccharomyces cerevisiae; Sp, Sacccharomyces paradoxus; Su, Sacccharomyces uvarum; Kl, Kluyveromyces lactis; Ca, Candida albicans; Spb, Schizosaccharomyces pombe; PrD, prion domain
¶ Corresponding author. E-mail address: Christophe.cullin{at}IBGC.U-Bordeaux2.fr.
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