Modulation of Aβ42 low-n oligomerization using a novel yeast reporter system

BMC Biology

Volumn 4, Issue , 2006, Pages

  Bagriantsev, Sviatoslav ^a   Liebman, Susan ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CHAPERONE; GUANIDINE; HEAT SHOCK PROTEIN 104; HYBRID PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSLATION TERMINATION FACTOR; TRANSLATION TERMINATION FACTOR SUP35; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; MACROMOLECULE; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ARTICLE; CELL CULTURE; CONTROLLED STUDY; DRUG SCREENING; GENE DISRUPTION; MAMMAL CELL; MODULATION; MUTATIONAL ANALYSIS; OLIGOMERIZATION; PATHOGENESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; GENETICS; MACROMOLECULE; MAMMAL; METABOLISM; PATHOPHYSIOLOGY; POINT MUTATION; REPORTER GENE;

MAMMALIA;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANIMALS; GENES, REPORTER; HEAT-SHOCK PROTEINS; MACROMOLECULAR SUBSTANCES; MAMMALS; MODELS, BIOLOGICAL; PEPTIDE FRAGMENTS; POINT MUTATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 33750010673     PISSN: 17417007     EISSN: 17417007     Source Type: Journal    
DOI: 10.1186/1741-7007-4-32     Document Type: Article

References (62)

1. LaFerla FM, Oddo S: Alzheimer's disease: Abeta, tau and synaptic dysfunction. Trends Mol Med 2005, 11:170-176.
2. Lesne S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M, Ashe KH: A specific amyloid-beta. protein assembly in the brain impairs memory. Nature 2006, 440:352-357.
3. Hardy J, Selkoe DJ: The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
4. Walsh DM, Selkoe DJ: Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 2004, 44:181-193.
5. Klein WL, Stine WB Jr, Teplow DB: Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 2004, 25:569-580.
6. LeVine H 3rd, Scholten JD: Screening for pharmacologic inhibitors of amyloid fibril formation. Methods Enzymol 1999, 309:467-476.
7. Soto C, Estrada L: Amyloid inhibitors and beta-sheet breakers. Subcell Biochem 2005, 38:351-364.
8. Fisher AC, Kim W, DeLisa MP: Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci 2006, 15:449-458.
9. Sherman MY, Muchowski PJ: Making yeast tremble: yeast models as tools to study neurodegenerative disorders. Neuromolecular Med 2003, 4:133-146.
10. Mager WH, Winderickx J: Yeast as a model for medical and medicinal research. Trends Pharmacol Sci 2005, 26:265-273.
11. Outeiro TF, Lindquist S: Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 2003, 302:1772-1775.
12. Willingham S, Outeiro TF, DeVit MJ, Lindquist SL, Muchowski PJ: Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 2003, 302:1769-1772.
13. Bach S, Talarek N, Andrieu T, Vierfond JM, Mettey Y, Galons H, Dormont D, Meijer L, Cullin C, Blondel M: Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol 2003, 21:1075-1081.
14. Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW: Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci USA 2004, 101:12934-12939.
15. Rochet JC, Outeiro TF, Conway KA, Ding TT, Volles MJ, Lashuel HA, Bieganski RM, Lindquist SL, Lansbury PT: Interactions among alpha-synuclein, dopamine, and blomembranes: some clues for understanding neurodegeneration in Parkinson's disease. J Mol Neurosci 2004, 23:23-34.
16. Zabrocki P, Pellens K, Vanhelmont T, Vandebroek T, Griffioen G, Wera S, Van Leuven F, Winderickx J: Characterization of alpha-synuclein aggregation and synergistic toxicity with protein tau in yeast. Febs J 2005, 272:1386-1400.
17. Vandebroek T, Vanhelmont T, Terwel D, Borghgraef P, Lemaire K, Snauwaert J, Wera S, Van Leuven F, Winderickx J: Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 2005, 44:11466-11475.
18. 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, 280:22809-22818.
19. +], and [Hets]". In Prion Biology and Diseases 2nd edition. Edited by: Prusiner SB. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; 2004:305-372.
20. Chien P, Weissman JS, DePace AH: Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004, 73:617-656.
21. Wickner RB, Edskes HK, Ross ED, Pierce MM, Baxa U, Brachmann A, Shewmaker F: Prion genetics: new rules for a new kind of gene. Annu Rev Genet 2004, 38:681-707.
22. Satpute-Krishnan P, Serio TR: Prion protein remodelling confers an immediate phenotypic switch. Nature 2005, 437:262-265.
23. Sanchez Y, Lindquist SL: HSP 104 required for induced thermotolerance. Science 1990, 248:1112-1115.
24. Lindquist S, Kim G: Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc Natl Acad Sci USA 1996, 93:5301-5306.
25. +]. Science 1995, 268:880-884.
26. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp 104. J Biol Chem 2003, 278:49636-49643.
27. Shorter J, Lindquist S: Hsp 104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004, 304:1793-1797.
28. Wegrzyn RD, Bapat K, Newnam GP, Zink AD, Chernoff YO: Mechanism of prion loss after Hsp 104 inactivation in yeast. Mol Cell Biol 2001, 21:4656-4669.
29. Ness F, Ferreira P, Cox BS, Tuite MF: Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 2002, 22:5593-5605.
30. Grimminger V, Richter K, Imhof A, Buchner J, Walter S: The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp 104. J Biol Chem 2004, 279:7378-7383.
31. Tuite MF, Mundy CR, Cox BS: Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 1981, 98:691-711.
32. Serio TR, Cashikar AG, Moslehi JJ, Kowal AS, Lindquist SL: Yeast prion [psi +] and its determinant, Sup35p. Methods Enzymol 1999, 309:649-673.
33. Chernoff YO, Uptain SM, Lindquist SL: Analysis of prion factors in yeast. Methods Enzymol 2002, 351:499-538.
34. Cox BS: [PSI], a cytoplasmic suppressor of super-suppression in yeast. Heredity 1965, 20:505-521.
35. Williams AD, Portelius E, Kheterpal I, Guo JT, Cook KD, Xu Y, Wetzel R: Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis. J. Mol Biol 2004, 335:833-842.
36. Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K: Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J Mol Biol 1992, 228:460-473.
37. Morimoto A, Irie K. Murakami K, Masuda Y, Ohigashi H, Nagao M, Fukuda H, Shimizu T, Shirasawa T: Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. J Biol Chem 2004, 279:52781-52788.
38. Palmert MR, Podlisny MB, Witker DS, Oltersdorf T, Younkin LH, Selkoe DJ, Younkin SG: The beta-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid. Proc Natl Acad Sci USA 1989, 86:6338-6342.
39. Podlisny MB, Walsh DM, Amarante P, Ostaszewski BL, Stimson ER, Maggio JE, Teplow DB, Selkoe DJ: Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 1998, 37:3602-3611.
40. Walsh DM, Tseng BP, Rydel RE, Podlisny MB, Sekoe DJ: The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 2000, 39:10831-10839.
41. Walsh DM, Selkoe DJ: Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 2004, 11:213-228.
42. Allen KD, Wegrzyn RD, Chernova TA, Muller S, Newnam GP, Winslett PA, Wittich KB, Wilkinson KD, Chernoff YO: Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 2005, 169:1227-1242.
43. Bagriantsev SN, Kushnirov VV, Liebman SW: Analysis of amyloid aggregates using agarose gel electrophoresis. Methods Enzymol 2006, 412:33-48. (in press).
44. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300:486-489.
45. Schirmer EC, Lindquist S: Interactions of the chaperone Hsp 104 with yeast Sup35 and mammalian PrP. Proc Natl Acad Sci USA 1997, 94:13932-13937.
46. Glover JR, Lindquist S: Hsp 104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
47. Cashikar AG, Duennwald M, Lindquist SL: A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp 104. J Biol Chem 2005, 280:23869-23875.
48. Haslbeck M, Miess A, Stromer T, Walter S, Buchner J: Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 2005, 280:23861-23868.
49. Muchowski PJ, Wacker JL: Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005, 6:11-22.
50. Parsell DA, Kowal AS, Singer MA, Lindquist S: Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994, 372:475-478.
51. Bukau B, Horwich AL: The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
52. Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hartl FU: Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc Natl Acad Sci USA 2000, 97:7841-7846.
53. Krobitsch S, Lindquist S: Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci USA 2000, 97:1589-1594.
54. Chernoff YO, Derkach IL, Inge-Vechtomov SG: Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 1993, 24:268-270.
55. Nakayashiki T, Ebihara K, Bannai H, Nakamura Y: Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol Cell 2001, 7:1121-1130.
56. Crist CG, Nakayashiki T, Kurahashi H, Nakamura Y: [PHI+], a novel Sup35-prion variant propagated with non-Gin/Asn oligopeptide repeats in the absence of the chaperone protein Hsp 104. Genes Cells 2003, 8:603-618.
57. Sherman F: Getting started with yeast. Methods Enzymol 2002, 350:3-41.
58. DePace AH, Santoso A, Hillner P, Weissman JS: A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 1998, 93:1241-1252.
59. Cormack BP, Valdivia RH, Falkow S: FACS-optimized mutants of the green fluorescent protein (GFP). Gene 1996, 173:33-38.
60. Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
61. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
62. Bagriantsev S, Liebman SW: Specificity of Prion Assembly in Vivo: [PSI+] and [PIN+] form separate structures in yeast. J Biol Chem 2004, 279:51042-51048.