QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 18, Issue 6, 2149-2154, June 2007

This Article Full Text Full Text (PDF) All Versions of this Article: E07-02-0128v1 18/6/2149    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kryndushkin, D. Articles by Wickner, R. B. Search for Related Content PubMed PubMed Citation Articles by Kryndushkin, D. Articles by Wickner, R. B.

Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae

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

Submitted February 15, 2007; Revised March 8, 2007; Accepted March 20, 2007
Monitoring Editor: Jonathan Weissman

The [URE3] and [PSI⁺] prions are infectious amyloid forms of Ure2p and Sup35p. Several chaperones influence prion propagation: Hsp104p overproduction destabilizes [PSI⁺], whereas [URE3] is sensitive to excess of Ssa1p or Ydj1p. Here, we show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3]. Sse1p and Fes1p are nucleotide exchange factors for Ssa1p. Interestingly, deletion of either SSE1 or FES1 completely blocked [URE3] propagation. In addition, deletion of SSE1 also interfered with [PSI⁺] propagation.

Address correspondence to: Reed B. Wickner (wickner{at}helix.nih.gov).

This article has been cited by other articles:

				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]

				J. Nemecek, T. Nakayashiki, and R. B. Wickner A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen PNAS, February 10, 2009; 106(6): 1892 - 1896. [Abstract] [Full Text] [PDF]

				J. A. Pezza, S. X. Langseth, R. Raupp Yamamoto, S. M. Doris, S. P. Ulin, A. R. Salomon, and T. R. Serio The NatA Acetyltransferase Couples Sup35 Prion Complexes to the [PSI+] Phenotype Mol. Biol. Cell, February 1, 2009; 20(3): 1068 - 1080. [Abstract] [Full Text] [PDF]

				C. Krammer, D. Kryndushkin, M. H. Suhre, E. Kremmer, A. Hofmann, A. Pfeifer, T. Scheibel, R. B. Wickner, H. M. Schatzl, and I. Vorberg From the Cover: The yeast Sup35NM domain propagates as a prion in mammalian cells PNAS, January 13, 2009; 106(2): 462 - 467. [Abstract] [Full Text] [PDF]

				D. Sharma, R. F. Stanley, and D. C. Masison Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70 Genetics, January 1, 2009; 181(1): 129 - 137. [Abstract] [Full Text] [PDF]

				S. N. Bagriantsev, E. O. Gracheva, J. E. Richmond, and S. W. Liebman Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition Mol. Biol. Cell, June 1, 2008; 19(6): 2433 - 2443. [Abstract] [Full Text] [PDF]

				Q. Fan, K.-W. Park, Z. Du, K. A. Morano, and L. Li The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion Genetics, November 1, 2007; 177(3): 1583 - 1593. [Abstract] [Full Text] [PDF]

				C. N. Martineau, J.-M. Beckerich, and M. Kabani Flo11p-Independent Control of "Mat" Formation by Hsp70 Molecular Chaperones and Nucleotide Exchange Factors in Yeast Genetics, November 1, 2007; 177(3): 1679 - 1689. [Abstract] [Full Text] [PDF]