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 Moriyama, H.
Right arrow Articles by Wickner, R. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moriyama, H.
Right arrow Articles by Wickner, R. B.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, December 2000, p. 8916-8922, Vol. 20, No. 23
0270-7306/00/$04.00+0

[URE3] Prion Propagation in Saccharomyces cerevisiae: Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p

Hiromitsu Moriyama, Herman K. Edskes, and Reed B. Wickner*

Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830

Received 3 July 2000/Returned for modification 29 August 2000/Accepted 11 September 2000

The [URE3] nonchromosomal genetic element is an infectious form (prion) of the Ure2 protein, apparently a self-propagating amyloidosis. We find that an insertion mutation or deletion of HSP104 results in inability to propagate the [URE3] prion. Our results indicate that Hsp104 is a common factor in the maintenance of two independent yeast prions. However, overproduction of Hsp104 does not affect the stability of [URE3], in contrast to what is found for the [PSI+] prion, which is known to be cured by either overproduction or deficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p, with the Hsp70 class Ssa1p, can renature proteins. We find that overproduction of Ydj1p results in a gradual complete loss of [URE3]. The involvement of protein chaperones in the propagation of [URE3] indicates a role for protein conformation in inheritance.

* Corresponding author. Mailing address: Bldg. 8, Room 225, N.I.H., 8 Center Dr. MSC0830, Bethesda, MD 20892-0830. Phone: (301) 496-3452. Fax: (301) 402-0240. E-mail: wickner{at}helix.nih.gov.

Molecular and Cellular Biology, December 2000, p. 8916-8922, Vol. 20, No. 23
0270-7306/00/$04.00+0


This article has been cited by other articles:

  • Brown, J. C.S., Lindquist, S. (2009). A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes Dev. 23: 2320-2332 [Abstract] [Full Text]  
  • Nemecek, J., Nakayashiki, T., Wickner, R. B. (2009). A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc. Natl. Acad. Sci. USA 106: 1892-1896 [Abstract] [Full Text]  
  • Ishiwata, M., Kurahashi, H., Nakamura, Y. (2009). A G-protein {gamma} subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 106: 791-796 [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]  
  • Lum, R., Niggemann, M., Glover, J. R. (2008). Peptide and Protein Binding in the Axial Channel of Hsp104: INSIGHTS INTO THE MECHANISM OF PROTEIN UNFOLDING. J. Biol. Chem. 283: 30139-30150 [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]  
  • Savistchenko, J., Krzewska, J., Fay, N., Melki, R. (2008). Molecular Chaperones and the Assembly of the Prion Ure2p in Vitro. J. Biol. Chem. 283: 15732-15739 [Abstract] [Full Text]  
  • Bagriantsev, S. N., Gracheva, E. O., Richmond, J. E., Liebman, S. W. (2008). Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition. Mol. Biol. Cell 19: 2433-2443 [Abstract] [Full Text]  
  • Malato, L., Dos Reis, S., Benkemoun, L., Sabate, R., Saupe, S. J. (2007). Role of Hsp104 in the Propagation and Inheritance of the [Het-s] Prion. Mol. Biol. Cell 18: 4803-4812 [Abstract] [Full Text]  
  • Shewmaker, F., Mull, L., Nakayashiki, T., Masison, D. C., Wickner, R. B. (2007). Ure2p Function Is Enhanced by Its Prion Domain in Saccharomyces cerevisiae. Genetics 176: 1557-1565 [Abstract] [Full Text]  
  • Kryndushkin, D., Wickner, R. B. (2007). Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae. Mol. Biol. Cell 18: 2149-2154 [Abstract] [Full Text]  
  • Lian, H.-Y., Zhang, H., Zhang, Z.-R., Loovers, H. M., Jones, G. W., Rowling, P. J. E., Itzhaki, L. S., Zhou, J.-M., Perrett, S. (2007). Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils. J. Biol. Chem. 282: 11931-11940 [Abstract] [Full Text]  
  • Immel, F., Jiang, Y., Wang, Y.-Q., Marchal, C., Maillet, L., Perrett, S., Cullin, C. (2007). In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion. J. Biol. Chem. 282: 7912-7920 [Abstract] [Full Text]  
  • Loovers, H. M., Guinan, E., Jones, G. W. (2007). Importance of the Hsp70 ATPase Domain in Yeast Prion Propagation. Genetics 175: 621-630 [Abstract] [Full Text]  
  • Hung, G.-C., Masison, D. C. (2006). N-Terminal Domain of Yeast Hsp104 Chaperone Is Dispensable for Thermotolerance and Prion Propagation but Necessary for Curing Prions by Hsp104 Overexpression. Genetics 173: 611-620 [Abstract] [Full Text]  
  • Wu, Y.-X., Greene, L. E., Masison, D. C., Eisenberg, E. (2005). Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division. Proc. Natl. Acad. Sci. USA 102: 12789-12794 [Abstract] [Full Text]  
  • Gokhale, K. C., Newnam, G. P., Sherman, M. Y., Chernoff, Y. O. (2005). Modulation of Prion-dependent Polyglutamine Aggregation and Toxicity by Chaperone Proteins in the Yeast Model. J. Biol. Chem. 280: 22809-22818 [Abstract] [Full Text]  
  • Song, Y., Wu, Y.-x., Jung, G., Tutar, Y., Eisenberg, E., Greene, L. E., Masison, D. C. (2005). Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication. Eukaryot Cell 4: 289-297 [Abstract] [Full Text]  
  • Tkach, J. M., Glover, J. R. (2004). Amino Acid Substitutions in the C-terminal AAA+ Module of Hsp104 Prevent Substrate Recognition by Disrupting Oligomerization and Cause High Temperature Inactivation. J. Biol. Chem. 279: 35692-35701 [Abstract] [Full Text]  
  • Kimura, Y., Koitabashi, S., Kakizuka, A., Fujita, T. (2004). The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. GENES CELLS 9: 685-696 [Abstract] [Full Text]  
  • Jones, G., Song, Y., Chung, S., Masison, D. C. (2004). Propagation of Saccharomyces cerevisiae [PSI+] Prion Is Impaired by Factors That Regulate Hsp70 Substrate Binding. Mol. Cell. Biol. 24: 3928-3937 [Abstract] [Full Text]  
  • Schirmer, E. C., Homann, O. R., Kowal, A. S., Lindquist, S. (2004). Dominant Gain-of-Function Mutations in Hsp104p Reveal Crucial Roles for the Middle Region. Mol. Biol. Cell 15: 2061-2072 [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]  
  • Grimminger, V., Richter, K., Imhof, A., Buchner, J., Walter, S. (2004). The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104. J. Biol. Chem. 279: 7378-7383 [Abstract] [Full Text]  
  • WICKNER, R.B., EDSKES, H.K., ROSS, E.D., PIERCE, M.M., SHEWMAKER, F., BAXA, U., BRACHMANN, A. (2004). Prions of Yeast Are Genes Made of Protein: Amyloids and Enzymes. Cold Spring Harb Symp Quant Biol 69: 489-496 [Abstract]  
  • Baudin-Baillieu, A., Fernandez-Bellot, E., Reine, F., Coissac, E., Cullin, C. (2003). Conservation of the Prion Properties of Ure2p through Evolution. Mol. Biol. Cell 14: 3449-3458 [Abstract] [Full Text]  
  • Rai, R., Tate, J. J., Cooper, T. G. (2003). Ure2, a Prion Precursor with Homology to Glutathione S-Transferase, Protects Saccharomyces cerevisiae Cells from Heavy Metal Ion and Oxidant Toxicity. J. Biol. Chem. 278: 12826-12833 [Abstract] [Full Text]  
  • Jones, G. W., Masison, D. C. (2003). Saccharomyces cerevisiae Hsp70 Mutations Affect [PSI+] Prion Propagation and Cell Growth Differently and Implicate Hsp40 and Tetratricopeptide Repeat Cochaperones in Impairment of [PSI+]. Genetics 163: 495-506 [Abstract] [Full Text]  
  • Ness, F., Ferreira, P., Cox, B. S., Tuite, M. F. (2002). Guanidine Hydrochloride Inhibits the Generation of Prion "Seeds" but Not Prion Protein Aggregation in Yeast. Mol. Cell. Biol. 22: 5593-5605 [Abstract] [Full Text]  
  • Lockshon, D. (2002). A Heritable Structural Alteration of the Yeast Mitochondrion. Genetics 161: 1425-1435 [Abstract] [Full Text]  
  • Jung, G., Jones, G., Masison, D. C. (2002). Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc. Natl. Acad. Sci. USA 99: 9936-9941 [Abstract] [Full Text]  
  • Kryndushkin, D. S., Smirnov, V. N., Ter-Avanesyan, M. D., Kushnirov, V. V. (2002). Increased Expression of Hsp40 Chaperones, Transcriptional Factors, and Ribosomal Protein Rpp0 Can Cure Yeast Prions. J. Biol. Chem. 277: 23702-23708 [Abstract] [Full Text]  
  • Meriin, A. B., Zhang, X., He, X., Newnam, G. P., Chernoff, Y. O., Sherman, M. Y. (2002). Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. JCB 157: 997-1004 [Abstract] [Full Text]  
  • Schwimmer, C., Masison, D. C. (2002). Antagonistic Interactions between Yeast [PSI+] and [URE3] Prions and Curing of [URE3] by Hsp70 Protein Chaperone Ssa1p but Not by Ssa2p. Mol. Cell. Biol. 22: 3590-3598 [Abstract] [Full Text]  
  • Hattendorf, D. A., Lindquist, S. L. (2002). Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc. Natl. Acad. Sci. USA 10.1073/pnas.261693199v1 [Abstract] [Full Text]  
  • Volkov, K. V., Aksenova, A. Yu., Soom, M. J., Osipov, K. V., Svitin, A. V., Kurischko, C., Shkundina, I. S., Ter-Avanesyan, M. D., Inge-Vechtomov, S. G., Mironova, L. N. (2002). Novel Non-Mendelian Determinant Involved in the Control of Translation Accuracy in Saccharomyces cerevisiae. Genetics 160: 25-36 [Abstract] [Full Text]  
  • Abbas-Terki, T., Donze, O., Briand, P.-A., Picard, D. (2001). Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast. Mol. Cell. Biol. 21: 7569-7575 [Abstract] [Full Text]  
  • Pierce, M. M., Maddelein, M.-L., Roberts, B. T., Wickner, R. B. (2001). A novel Rtg2p activity regulates nitrogen catabolism in yeast. Proc. Natl. Acad. Sci. USA 10.1073/pnas.181486098v1 [Abstract] [Full Text]  
  • Schlumpberger, M., Prusiner, S. B., Herskowitz, I. (2001). Induction of Distinct [URE3] Yeast Prion Strains. Mol. Cell. Biol. 21: 7035-7046 [Abstract] [Full Text]  
  • Wegrzyn, R. D., Bapat, K., Newnam, G. P., Zink, A. D., Chernoff, Y. O. (2001). Mechanism of Prion Loss after Hsp104 Inactivation in Yeast. Mol. Cell. Biol. 21: 4656-4669 [Abstract] [Full Text]  
  • Speransky, V. V., Taylor, K. L., Edskes, H. K., Wickner, R. B., Steven, A. C. (2001). Prion Filament Networks in [Ure3] Cells of Saccharomyces cerevisiae. JCB 153: 1327-1336 [Abstract] [Full Text]  
  • Pierce, M. M., Maddelein, M.-L., Roberts, B. T., Wickner, R. B. (2001). A novel Rtg2p activity regulates nitrogen catabolism in yeast. Proc. Natl. Acad. Sci. USA 98: 13213-13218 [Abstract] [Full Text]  
  • Hattendorf, D. A., Lindquist, S. L. (2002). Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc. Natl. Acad. Sci. USA 99: 2732-2737 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»