Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ+] prion

Prion

Volumn 3, Issue 3, 2009, Pages 151-160

  Bardill, J Patrick ^a,b   Dulle, Jennifer E ^a   Fisher, Jonathan R ^a   True, Heather L ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Hsp104p; Mutagenesis; Sis1p; PSI+ ; RNQ+

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; CHAPERONE PROTEIN SIS 1P; GLUTAMIC ACID; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 104P; LYSINE; PROTEIN; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HSP104 PROTEIN, S CEREVISIAE; HYBRID PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SIS1 PROTEIN, S CEREVISIAE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL LOSS; CONTROLLED STUDY; GENE CONSTRUCT; GENE EXPRESSION; GENE MUTATION; GENETIC SCREENING; HEAT TOLERANCE; HYDROLYSIS; IN VIVO STUDY; MUTANT; NONHUMAN; PRION; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN INDUCTION; PROTEIN PURIFICATION; REPORTER GENE; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; VIRUS STRAIN; WILD TYPE; BIOLOGICAL MODEL; CHEMISTRY; HEAT; METABOLISM; MUTATION; PHENOTYPE; PHYSIOLOGY; TEMPERATURE;

SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; HEAT-SHOCK PROTEINS; HOT TEMPERATURE; HSP40 HEAT-SHOCK PROTEINS; HYDROLYSIS; MODELS, GENETIC; MOLECULAR CHAPERONES; MUTATION; PHENOTYPE; PRIONS; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE;

EID: 70349780021     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.3.3.9662     Document Type: Article

References (63)

1. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24:519-50.
2. Wickner RB, Masison DC, Edskes HK. [PSI] and [URE3] as yeast prions. Yeast 1995; 11:1671-85.
3. Du Z, Park KW, Yu H, Fan Q, Li L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 2008; 40:460-5.
4. Patel BK, Gavin-Smyth J, Liebman SW. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 2009.
5. Tyedmers J, Madariaga ML, Lindquist S. Prion switching in response to environmental stress. PLoS Biol 2008; 6:294.
6. True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477-83.
7. True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184-7. Epub 2004.
8. Eaglestone SS, Cox BS, Tuite MF. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J 1999; 18:1974-81.
9. +] prion in Saccharomyces cerevisiae. Genetics 1997; 147:507-19.
10. Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, Inge-Vechtomov SG, et al. Dependence and independence of [PSI(+)] and [PIN(+)]: a twoprion system in yeast? EMBO J 2000; 19:1942-52.
11. Sondheimer N, Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 2000; 5:163-72.
12. Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 2001; 106:183-94.
13. Jones GW, Tuite MF. Chaperoning prions: the cellular machinery for propagating an infectious protein? Bioessays 2005; 27:823-32.
14. True HL. The battle of the fold: chaperones take on prions. Trends Genet 2006; 22:110-7.
15. Lindquist S, Kim G. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc Natl Acad Sci USA 1996; 93:5301-6.
16. Sanchez Y, Taulien J, Borkovich KA, Lindquist S. Hsp104 is required for tolerance to many forms of stress. EMBO J 1992; 11:2357-64.
17. Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004; 304:1793-7.
18. Glover JR, Lindquist S. Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998; 94:73-82.
19. Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, et al. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 2003; 115:229-40.
20. Hung GC, Masison DC. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics 2006; 173:611-20.
21. + module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J Biol Chem 2004; 279:35692-701.
22. Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994; 372:475-8.
23. Hattendorf DA, Lindquist SL. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J 2002; 21:12-21.
24. Hattendorf DA, Lindquist SL. 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 2002; 99:2732-7.
25. +]. Science 1995; 268:880-4.
26. Schirmer EC, Homann OR, Kowal AS, Lindquist S. Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol Biol Cell 2004; 15:2061-72.
27. Cashikar AG, Schirmer EC, Hattendorf DA, Glover JR, Ramakrishnan MS, Ware DM, et al. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell 2002; 9:751-60.
28. +] prion propagation in S. cerevisiae by comprehensive chromosomal mutations. Prion 2007; 1:69-77.
29. Kurahashi H, Nakamura Y. Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation. Mol Microbiol 2007; 63:1669-83.
30. Jung G, Jones G, Masison DC. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation and thermotolerance. Proc Natl Acad Sci USA 2002; 99:9936-41.
31. +], a heritable prion-like factor of S. cerevisiae. Cell 1997; 89:811-9.
32. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 2003; 278:49636-43.
33. +] seeds necessary for prion propagation. EMBO J 2007; 26:3794-803.
34. Wegrzyn RD, Bapat K, Newnam GP, Zink AD, Chernoff YO. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol 2001; 21:4656-69.
35. Moriyama H, Edskes HK, Wickner RB. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Molecular & Cellular Biology 2000; 20:8916-22.
36. Schwimmer C, Masison DC. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol Cell Biol 2002; 22:3590-8.
37. Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol 1999; 19:1325-33.
38. Allen KD, Wegrzyn RD, Chernova TA, Muller S, Newnam GP, Winslett PA, et al. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 2005; 169:1227-42.
39. +] and their prion-specific effects. Curr Biol 2000; 10:1443-6.
40. Bradley ME, Edskes HK, Hong JY, Wickner RB, Liebman SW. Interactions among prions and prion "strains" in yeast. Proc Natl Acad Sci USA 2002; 30:30.
41. Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andreasson C, Lindquist S, et al. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 2008; 3:1763.
42. Kryndushkin D, Wickner RB. Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae. Mol Biol Cell 2007; 18:2149-54.
43. +] Are Regulated by the Heat-Shock Transcription Factor. Genetics 2006; 173:35-47.
44. +] prion. EMBO J 2001; 20:2435-42.
45. Lopez N, Aron R, Craig EA. Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. Mol Biol Cell 2003; 14:1172-81.
46. Qian X, Hou W, Zhengang L, Sha B. Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 2002; 361:27-34.
47. Aron R, Lopez N, Walter W, Craig EA, Johnson J. In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 2005; 169:1873-82.
48. Higurashi T, Hines JK, Sahi C, Aron R, Craig EA. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci USA 2008; 105:16596-601.
49. Guthrie C, Fink G. Guide to Yeast Genetics and Molecular Biology. Vol 194. San Diego: Academic Press, Inc 1991.
50. Bardill JP, True HL. Heterologous prion interactions are altered by mutations in the prion protein Rnq1p. J Mol Biol 2009; 388:583-96.
51. Sikorski RS, Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 1989; 122:19-27.
52. +] prions in yeast. Methods 2006; 39:23-34.
53. Sanchez Y, Lindquist SL. HSP104 required for induced thermotolerance. Science 1990; 248:1112-5.
54. Schirmer EC, Queitsch C, Kowal AS, Parsell DA, Lindquist S. The ATPase activity of Hsp104, effects of environmental conditions and mutations. J Biol Chem 1998; 273:15546-52.
55. Parsell DA, Kowal AS, Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem 1994; 269:4480-7.
56. Ter-Avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, Inge-Vechtomov SG, et al. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 1993; 7:683-92.
57. Salnikova AB, Kryndushkin DS, Smirnov VN, Kushnirov VV, Ter-Avanesyan MD. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 2005; 280:8808-12.
58. Douglas PM, Treusch S, Ren HY, Halfmann R, Duennwald ML, Lindquist S, et al. Chaperonedependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci USA 2008; 105:7206-11.
59. Schirmer EC, Ware DM, Queitsch C, Kowal AS, Lindquist SL. Subunit interactions influence the biochemical and biological properties of Hsp104. Proc Natl Acad Sci USA 2001; 98:914-9. Epub 2001.
60. Gokhale KC, Newnam GP, Sherman MY, Chernoff YO. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 2005; 280:22809-18.
61. +] are diseases. Proc Natl Acad Sci USA 2005; 102:10575-80. Epub 2005.
62. Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001; 106:171-82.
63. +] form separate structures in yeast. J Biol Chem 2004; 279:51042-8.