J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation

EMBO Journal

Volumn 26, Issue 16, 2007, Pages 3794-3803

  Aron, Rebecca ^a,b,c   Higurashi, Takashi ^a   Sahi, Chandan ^a   Craig, Elizabeth A ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

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

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

PIN+ ; AAA+ ATPase; Hsp104; Hsp40; Hsp70

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; CHAPERONE SIS1; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 70; J PROTEIN; PROTEIN; RNQ1 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CELL POPULATION; CONFORMATION; CYTOSOL; GENE DELETION; PRION; PRIORITY JOURNAL; PROTEIN SYNTHESIS;

HEAT-SHOCK PROTEINS; PEPTIDE INITIATION FACTORS; PRIONS; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 34548101963     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601811     Document Type: Article

References (45)

1. +] form separate structures in yeast. J Biol Chem 279: 51042-51048
2. Borchsenius AS, Muller S, Newnam GP, Inge-Vechtomov SG, Chernoff YO (2006) Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet 49: 21-29
3. Bosl B, Grimminger V, Walter S (2006) The molecular chaperone Hsp104 - a molecular machine for protein disaggregation. J Struct Biol 156: 139-148
4. Brachmann A, Baxa U, Wickner RB (2005) Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 24: 3082-3092
5. Bradley ME, Bagriantsev S, Vishveshwara N, Liebman SW (2003) Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45. Yeast 20: 625-632
6. Campbell RE, Tour O, Palmer AE, Steinbach PA, Baird GS, Zacharias DA, Tsien RY (2002) A monomeric red fluorescent protein. Proc Natl Acad Sci USA 99: 7877-7882
7. +]. Science 268: 880-884
8. Conde J, Fink GR (1976) A mutant of Saccharomyces cerevisiae defective for nuclear fusion. Proc Natl Acad Sci USA 73: 3651-3655
9. Craig EA, Huang P, Aron R, Andrew A (2006) The diverse roles of J-proteins, the obligate Hsp70 co-chaperone. Rev Physiol Biochem Pharmacol 156: 1-21
10. Derkatch IL, Bradley ME, Hong JY, Liebman SW (2001) Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106: 171-182
11. +] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol 40: 1357-1369
12. Gari E, Piedrafita L, Aldea M, Herrero E (1997) A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae. Yeast 13: 837-848
13. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS (2003) Global analysis of protein expression in yeast. Nature 425: 737-741
14. +], a heritable prion-like factor of S. cerevisiae. Cell 89: 811-819
15. Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82
16. Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96: 13732-13737
17. 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
18. Heim R, Cubitt AB, Tsien RY (1995) Improved green fluorescence. Nature 373: 663-664
19. Jung G, Masison DC (2001) Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol 43: 7-10
20. King CY, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428: 319-323
21. King CY, Tittmann P, Gross H, Gebert R, Aebi M, Wuthrich K (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci USA 94: 6618-6622
22. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278: 49636-49643
23. Krzewska J, Langer T, Liberek K (2001) Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 489: 92-96
24. +]. Mol Biol Cell 14: 1172-1181
25. Motohashi K, Watanabe Y, Yohda M, Yoshida M (1999) Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci USA 96: 7184-7189
26. Mumberg D, Muller R, Funk M (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res 22: 5767-5768
27. Mumberg D, Muller R, Funk M (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156: 119-122
28. Ness F, Ferreira P, Cox BS, Tuite MF (2002) Guanidine hydrochloride inhibits the generation of prion 'seeds' but not prion protein aggregation in yeast. Mol Cell Biol 22: 5593-5605
29. Osherovich LZ, Weissman JS (2001) Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 106: 183-194
30. +]. J Mol Biol 365: 773-782
31. +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 15: 3127-3134
32. Satpute-Krishnan P, Langseth SX, Serio TR (2007) Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol 5: e24
33. Shorter J, Lindquist S (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797
34. Sikorski RS, Hieter P (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27
35. Sondheimer N, Lindquist S (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5: 163-172
36. +] prion. EMBO J 20: 2435-2442
37. Tanaka M, Chien P, Naber N, Cooke R, Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328
38. Tanaka M, Collins SR, Toyama BH, Weissman JS (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442: 585-589
39. Tsien RY (1998) The green fluorescent protein. Annu Rev Biochem 67: 509-544
40. Wegrzyn RD, Bapat K, Newnam GP, Zink AD, Chernoff YO (2001) Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol 21: 4656-4669
41. Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119: 653-665
42. Yan W, Craig EA (1999) The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol Cell Biol 19: 7751-7758
43. Zacharias DA, Violin JD, Newton AC, Tsien RY (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296: 913-916
44. Zietkiewicz S, Krzewska J, Liberek K (2004) Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem 279: 44376-44383
45. Zolkiewski M (1999) ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multichaperone system from Escherichia coli. J Biol Chem 274: 28083-28086