The role of Sis1 in the maintenance of the [RNQ+] prion

EMBO Journal

Volumn 20, Issue 10, 2001, Pages 2435-2442

  Sondheimer, Neal ^a   Lopez, Nelson ^b   Craig, Elizabeth A ^c   Lindquist, Susan ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

Chaperone; Prion; Rnq1; Sis1; Yeast

Indexed keywords

HEAT SHOCK PROTEIN 40; PRION PROTEIN; PROTEIN SIS1; UNCLASSIFIED DRUG;

ARTICLE; CHIMERA; DELETION MUTANT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN VARIANT;

ADENOSINE TRIPHOSPHATASES; FUNGAL PROTEINS; GREEN FLUORESCENT PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LUMINESCENT PROTEINS; MUTAGENESIS; PRIONS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0035873740     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.10.2435     Document Type: Article

References (30)

1. Bukau, B., Schmid, F. and Buchner, J. (1999) Assisted protein folding. In Bukau, B. (ed.), Molecular Chaperones and Folding Catalysts. Harwood Academic, Amsterdam, The Netherlands.
2. Chai, Y., Koppenhafer, S.L., Bonini, N.M. and Paulson, H.L. (1999) Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci., 19, 10338-10347.
3. Cheetham, M. and Caplan, A. (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones, 3, 28-36.
4. Chernoff, Y.O., Derkatch, I.L. and Inge-Vechtomov, S.G. (1993) Multicopy sup35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet., 24, 268-270.
5. +]. Science, 268, 880-884.
6. Chernoff, Y.O., Newnam, G.P., Kumar, J., Allen, K. and Zink, A.D. (1999) Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability and toxicity of the [PSI] prion. Mol. Cell. Biol., 19, 8103-8112.
7. Conde, J. and Fink, G.R. (1976) A mutant of Saccharomyces cerevisiae defective for nuclear fusion. Proc. Natl Acad. Sci. USA, 73, 3651-3655.
8. Craig, E., Yan, W. and James, P. (1999) Genetic dissection of the Hsp70 chaperone system of yeast. In Bukau, B. (ed.), Molecular Chaperones and Folding Catalysts. Harwood Academic, Amsterdam, The Netherlands, pp. 139-162.
9. Derkatch, I.L., Chernoff, Y.O., Kushnirov, V.V., Inge-Vechtomov, S.G. and Liebman, S.W. (1996) Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics, 144, 1375-1386.
10. Glover, J.R. and Lindquist, S. (1998) Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell, 94, 73-82.
11. Johnson, J.L. and Craig, E.A. (2001) An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol., 152, 851-856.
12. +] as a cellular stress. Genetics, 156, 559-570.
13. +] and their prion-specific effects. Curr. Biol., 10, 1443-1446.
14. Lu, Z. and Cyr, D.M. (1998) Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem., 273, 27824-27830.
15. Luke, M.M., Sutton, A. and Arndt, K.T. (1991) Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial DnaJ proteins. J. Cell Biol., 114, 623-638.
16. Moriyama, H., Edskes, H.K. and Wickner, R.B. (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1. Mol. Cell. Biol., 20, 8916-8922.
17. Newnam, G.P., Wegrzyn, R.D., Lindquist, S.L. and Chernoff, Y.O. (1999) Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol., 19, 1325-1333.
18. Parsell, D.A., Kowal, A.S., Singer, M.A. and Lindquist, S. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature, 372, 475-478.
19. Sanchez, Y. and Lindquist, S.L. (1990) Hsp104 required for induced thermotolerance. Science, 248, 1112-1115.
20. Sanchez, Y., Parsell, D.A., Taulien, J., Vogel, J.L., Craig, E.A. and Lindquist, S. (1993) Genetic evidence for a functional relationship between Hsp104 and Hsp70. J. Bacteriol., 175, 6484-6491.
21. +] in yeast by hypertonic media. Proc. Natl Acad. Sci. USA, 76, 1952-1956.
22. Sondheimer, N. (2000) The identification of novel prion elements in the yeast Saccharomyces cerevisiae. Doctoral dissertation. University of Chicago, Chicago, IL, pp. 1-161.
23. Sondheimer, N. and Lindquist, S. (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell, 5, 163-172.
24. True, H. and Lindquist, S. (2000) A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature, 407, 477-483.
25. Wach, A. (1996) PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast, 12, 259-265.
26. Wickner, R.B. (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science, 264, 566-569.
27. Wickner, R. and Chernoff, Y. (1999) Prions of fungi: [URE3], [PSI] and [Het-s] discovered as heritable traits. In Prusiner, S. (ed.), Prion Biology and Diseases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 229-272.
28. Yan, W. and Craig, E.A. (1999) The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol. Cell. Biol., 19, 7751-7758.
29. Zhong, T. and Arndt, K.T. (1993) The yeast Sis1 protein, a Dnaj homologue, is required for the initiation of translation. Cell, 73, 1175-1186.
30. +], a prion-like form of release factor eRF3. EMBO J., 18, 1182-1191.