This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schlumpberger, M.
Right arrow Articles by Herskowitz, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schlumpberger, M.
Right arrow Articles by Herskowitz, I.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2001, p. 7035-7046, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.7035-7046.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Induction of Distinct [URE3] Yeast Prion Strains

Martin Schlumpberger,1,2 Stanley B. Prusiner,1,2,3,* and Ira Herskowitz3

Institute for Neurodegenerative Diseases1 and Departments of Neurology2 and Biochemistry and Biophysics,3 University of California, San Francisco, California 94143-0518

Received 7 May 2001/Returned for modification 4 June 2001/Accepted 18 July 2001

[URE3] is a non-Mendelian genetic element in Saccharomyces cerevisiae, which is caused by a prion-like, autocatalytic conversion of the Ure2 protein (Ure2p) into an inactive form. The presence of [URE3] allows yeast cells to take up ureidosuccinic acid in the presence of ammonia. This phenotype can be used to select for the prion state. We have developed a novel reporter, in which the ADE2 gene is controlled by the DAL5 regulatory region, which allows monitoring of Ure2p function by a colony color phenotype. Using this reporter, we observed induction of different [URE3] prion variants ("strains") following overexpression of the N-terminal Ure2p prion domain (UPD) or full-length Ure2p. Full-length Ure2p induced two types of [URE3]: type A corresponds to conventional [URE3], whereas the novel type B variant is characterized by relatively high residual Ure2p activity and efficient curing by coexpression of low amounts of a UPD-green fluorescent protein fusion protein. Overexpression of UPD induced type B [URE3] but not type A. Both type A and B [URE3] strains, as well as weak and strong isolates of type A, were shown to stably maintain different prion strain characteristics. We suggest that these strain variants result from different modes of aggregation of similar Ure2p monomers. We also demonstrate a procedure to counterselect against the [URE3] state.


* Corresponding author. Mailing address: Institute for Neurodegenerative Diseases, Box 0518, University of California, San Francisco, CA 94143-0518. Phone: (415) 476-4482. Fax: (415) 476-8386. E-mail: stanley{at}itsa.ucsf.edu.


Molecular and Cellular Biology, October 2001, p. 7035-7046, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.7035-7046.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Choe, Y.-J., Ryu, Y., Kim, H.-J., Seok, Y.-J. (2009). Increased [PSI+] Appearance by Fusion of Rnq1 with the Prion Domain of Sup35 in Saccharomyces cerevisiae. Eukaryot Cell 8: 968-976 [Abstract] [Full Text]  
  • Edskes, H. K., McCann, L. M., Hebert, A. M., Wickner, R. B. (2009). Prion Variants and Species Barriers Among Saccharomyces Ure2 Proteins. Genetics 181: 1159-1167 [Abstract] [Full Text]  
  • Sharma, D., Stanley, R. F., Masison, D. C. (2009). Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70. Genetics 181: 129-137 [Abstract] [Full Text]  
  • Higurashi, T., Hines, J. K., Sahi, C., Aron, R., Craig, E. A. (2008). Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc. Natl. Acad. Sci. USA 105: 16596-16601 [Abstract] [Full Text]  
  • Sharma, D., Masison, D. C. (2008). Functionally Redundant Isoforms of a Yeast Hsp70 Chaperone Subfamily Have Different Antiprion Effects. Genetics 179: 1301-1311 [Abstract] [Full Text]  
  • Alexandrov, I. M., Vishnevskaya, A. B., Ter-Avanesyan, M. D., Kushnirov, V. V. (2008). Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION. J. Biol. Chem. 283: 15185-15192 [Abstract] [Full Text]  
  • Fan, Q., Park, K.-W., Du, Z., Morano, K. A., Li, L. (2007). The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion. Genetics 177: 1583-1593 [Abstract] [Full Text]  
  • Sen, A., Baxa, U., Simon, M. N., Wall, J. S., Sabate, R., Saupe, S. J., Steven, A. C. (2007). Mass Analysis by Scanning Transmission Electron Microscopy and Electron Diffraction Validate Predictions of Stacked beta-Solenoid Model of HET-s Prion Fibrils. J. Biol. Chem. 282: 5545-5550 [Abstract] [Full Text]  
  • Park, K.-W., Hahn, J.-S., Fan, Q., Thiele, D. J., Li, L. (2006). De Novo Appearance and "Strain" Formation of Yeast Prion [PSI+] Are Regulated by the Heat-Shock Transcription Factor. Genetics 173: 35-47 [Abstract] [Full Text]  
  • Talarek, N., Maillet, L., Cullin, C., Aigle, M. (2005). The [URE3] Prion Is Not Conserved Among Saccharomyces Species. Genetics 171: 23-34 [Abstract] [Full Text]  
  • Ripaud, L., Maillet, L., Immel-Torterotot, F., Durand, F., Cullin, C. (2004). The [URE3] Yeast Prion Results from Protein Aggregates That Differ from Amyloid Filaments Formed in Vitro. J. Biol. Chem. 279: 50962-50968 [Abstract] [Full Text]  
  • Wickner, R. B., Edskes, H. K., Roberts, B. T., Baxa, U., Pierce, M. M., Ross, E. D., Brachmann, A. (2004). Prions: proteins as genes and infectious entities. Genes Dev. 18: 470-485 [Full Text]  
  • Liebman, S. W. (2002). Progress toward an ultimate proof of the prion hypothesis. Proc. Natl. Acad. Sci. USA 99: 9098-9100 [Full Text]  
  • Baxa, U., Speransky, V., Steven, A. C., Wickner, R. B. (2002). Inaugural Article: Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc. Natl. Acad. Sci. USA 99: 5253-5260 [Abstract] [Full Text]  
  • Gueldener, U., Heinisch, J., Koehler, G. J., Voss, D., Hegemann, J. H. (2002). A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res 30: e23-e23 [Abstract] [Full Text]