- THIS ARTICLE
- Full Text
- Full Text (PDF)
- Supplemental Data
-
All Versions of this Article:
genetics.105.043489v1
171/1/23 most recent - Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Email this article to a friend
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Talarek, N.
- Articles by Aigle, M.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Talarek, N.
- Articles by Aigle, M.
Originally published as Genetics Published Articles Ahead of Print on June 14, 2005.
Genetics, Vol. 171, 23-34, September 2005, Copyright © 2005
doi:10.1534/genetics.105.043489
The [URE3] Prion Is Not Conserved Among Saccharomyces Species
Nicolas Talarek1, Laurent Maillet, Christophe Cullin and Michel Aigle
IBGC-CNRS/Université Victor Segalen Bordeaux2, UMR 5095, 33077 Bordeaux, France
1 Corresponding author: Dana-Farber Cancer Institute, M620, 44 Binney St., Boston, MA 02115.
E-mail: nicolas_talarek{at}dfci.harvard.edu
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.
This article has been cited by other articles:
 |
|
 |
|
  M. Crapeau, C. Marchal, C. Cullin, and L. Maillet The Cellular Concentration of the Yeast Ure2p Prion Protein Affects Its Propagation as a Prion Mol. Biol. Cell, April 15, 2009; 20(8): 2286 - 2296. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. K. Edskes, L. M. McCann, A. M. Hebert, and R. B. Wickner Prion Variants and Species Barriers Among Saccharomyces Ure2 Proteins Genetics, March 1, 2009; 181(3): 1159 - 1167. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. H. Wong, M. J. Hynes, and M. A. Davis Recent Advances in Nitrogen Regulation: a Comparison between Saccharomyces cerevisiae and Filamentous Fungi Eukaryot. Cell, June 1, 2008; 7(6): 917 - 925. [Full Text] [PDF]
|
|
|
|
|
|
F. Shewmaker, L. Mull, T. Nakayashiki, D. C. Masison, and R. B. Wickner Ure2p Function Is Enhanced by Its Prion Domain in Saccharomyces cerevisiae Genetics, July 1, 2007; 176(3): 1557 - 1565. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Immel, Y. Jiang, Y.-Q. Wang, C. Marchal, L. Maillet, S. Perrett, and C. Cullin In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion J. Biol. Chem., March 16, 2007; 282(11): 7912 - 7920. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Chen, G. P. Newnam, and Y. O. Chernoff Prion species barrier between the closely related yeast proteins is detected despite coaggregation PNAS, February 20, 2007; 104(8): 2791 - 2796. [Abstract] [Full Text] [PDF]
|
|