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A more recent version of this article appeared on August 1, 2003
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Submitted on January 15, 2003
Revised on April 4, 2003
Accepted on April 9, 2003
1 CGM, avenue de la Terrasse, 91190 Gif-sur-Yvette Cedex, France
2 Department of Biosciences, University of Kent at Canterbury, Canterbury, Kent CT2 7NJ, UK
3 IJM, 2 place Jussieu - 75251 Paris cedex 05 - France
4 IBGC, 1 , rue Camille Saint Saens 33077 Bordeaux cedex
* Corresponding author. E-mail address: Christophe.cullin{at}IBGC.U-Bordeaux2.fr.
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: S. paradoxus, S. uvarum, K. lactis, C. albicans and S. 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.
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