The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils

Journal of Structural Biology

Volumn 141, Issue 2, 2003, Pages 132-142

  Bousset, Luc ^a   Briki, Fatma ^b   Doucet, Jean ^b,c   Melki, Ronald ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

Amyloid fibrils; Assembly; Conformational transition; Prion; Saccharomyces cerevisiae; Ure2p; X ray fiber diffraction

Indexed keywords

AMYLOID; PROTEIN; PROTEIN URE2P; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FIBER; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SPECTROSCOPY; X RAY DIFFRACTION;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0037291995     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00606-8     Document Type: Article

References (46)

1. Astbury W.T., Woods H.J. Philos. Trans. A. 232:1933;333-394.
2. Balbirnie M., Grothe R., Eisenberg D.S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA. 98:2001;2375-2380.
3. Blake C., Serpell L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure. 4:1996;989-998.
4. Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S., Schulte G.K., Danley D.E., Hoth L.R., Griffor M.C., Kamath A.V., Rosner M.H., Chrunyk B.A., Perregaux D.E., Gabel C.A., Geoghegan K.F., Pandit J. Identification, characterization, and crystal structure of the Ω class glutathione transferases. J. Biol. Chem. 275:2000;24798-24806.
5. Bolton D.C., McKinley M.P., Prusiner S.B. Identification of a protein that purifies with the scrapie prion. Science. 218:1982;1309-1311.
6. Bousset L., Belrhali H., Janin J., Melki R., Morera S. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure (Camb). 9:2001;39-46.
7. Bousset L., Belrhali H., Melki R., Morera S. Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry. 40:2001;13564-13573.
8. Bousset L., Melki R. Similar and divergent features in mammalian and yeast prions. Microbes Infect. 4:2002;461-469.
9. Bousset L., Thomson N.H., Radford S.E., Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21:2002;2903-2911.
10. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
11. Carrell R.W., Gooptu B. Conformational changes and disease - serpins, prions, and Alzheimer's. Curr. Opin. Struct. Biol. 8:1998;799-809.
12. Cox B.S. PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity. 20:1965;505-521.
13. Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell. 106:2001;171-182.
14. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
15. Edskes H.K., Gray V.T., Wickner R.B. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. USA. 96:1999;1498-1503.
16. Fandrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature. 410:2001;165-166.
17. Fernandez-Bellot E., Guillemet E., Cullin C. The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J. 19:2000;3215-3222.
18. Garson J.C., Doucet J., Leveque J.L., Tsoucaris G. Oriented structure in human stratum corneum revealed by X-ray diffraction. J. Invest. Dermatol. 96:1991;43-49.
19. Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 89:1997;811-819.
20. Jimenez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:1999;815-821.
21. Jimenez J.L., Nettleton E.J., Bouchard M., Robinson C.V., Dobson C.M., Saibil H.R. The protofilament structure of insulin amyloid fibrils. Proc. Natl. Acad. Sci. USA. 99:2002;9196-9201.
22. Kad N.M., Thomson N.H., Smith D.P., Smith D.A., Radford S.E. β(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J. Mol. Biol. 313:2001;559-571.
23. Khurana R., Uversky V.N., Neilsen L., Fink A.L. Is Congo red an amyloid-specific dye. J. Biol. Chem. 276:2001;22715-22721.
24. Kirschner D.A., Abraham C., Selkoe D.J. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl. Acad. Sci. USA. 83:1986;503-507.
25. Krebs M.R., Wilkins D.K., Chung E.W., Pitkeathly M.C., Chamberlain A.K., Zurdo J., Robinson C.V., Dobson C.M. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain. J. Mol. Biol. 300:2000;541-549.
26. Lacroute F. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106:1971;519-522.
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
28. Lim A., Makhov A.M., Bond J., Inouye H., Connors L.H., Griffith J.D., Erickson B.W., Kirschner D.A., Costello C.E. Betabellins 15D and 16D, de novo designed β-sandwich proteins that have amyloidogenic properties. J. Struct. Biol. 130:2000;363-370.
29. Magasanik B. The Molecular and Cellular Biology of the Yeast Saccharomyces cerevisiae. 1992;Cold Spring Harbor Laboratory Press, Plainview, NY.
30. Masison D.C., Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science. 270:1995;93-95.
31. McParland V.J., Kad N.M., Kalverda A.P., Brown A., Kirwin-Jones P., Hunter M.G., Sunde M., Radford S.E. Partially unfolded states of β(2)-microglobulin and amyloid formation in vitro. Biochemistry. 39:2000;8735-8746.
32. Morozova-Roche L.A., Zurdo J., Spencer A., Noppe W., Receveur V., Archer D.B., Joniau M., Dobson C.M. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130:2000;339-351.
33. Perutz M.F., Pope B.J., Owen D., Wanker E.E., Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc. Natl. Acad. Sci. USA. 99:2002;5596-5600.
34. Polack F., Mercier R., Nahon L., Armellin C., Marx J.P., Tanguy M., Couprie M.E., P.D Optical design and performances of the IR microscope beamline at SuperACO. Carr G.L., Dumas P. SPIE Proceedings (1999), Paris, France. 1999.
35. Santoso A., Chien P., Osherovich L.Z., Weissman J.S. Molecular basis of a yeast prion species barrier. Cell. 100:2000;277-288.
36. Schlumpberger M., Prusiner S.B., Herskowitz I. Induction of distinct [URE3] yeast prion strains. Mol. Cell. Biol. 21:2001;7035-7046.
37. Sondheimer N., Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell. 5:2000;163-172.
38. Stuart B. Biological application of Infrared Spectroscopy. 1997;Wiley, Sydney, Australia.
39. Sunde M., Serpell L.C., Bartlam M., Fraser P.E., Pepys M.B., Blake C.C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273:1997;729-739.
40. Taylor K.L., Cheng N., Williams R.W., Steven A.C., Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science. 283:1999;1339-1343.
41. Thual C., Bousset L., Komar A.A., Walter S., Buchner J., Cullin C., Melki R. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry. 40:2001;1764-1773.
42. Thual C., Komar A.A., Bousset L., Fernandez-Bellot E., Cullin C., Melki R. Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J. Biol. Chem. 274:1999;13666-13674.
43. Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA. 98:2001;1459-1464.
44. Uptain S.M., Sawicki G.J., Caughey B., Lindquist S. Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J. 20:2001;6236-6245.
45. Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 264:1994;566-569.
46. Wille H., Michelitsch M.D., Guenebaut V., Supattapone S., Serban A., Cohen F.E., Agard D.A., Prusiner S.B. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. USA. 99:2002;3563-3568.