β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers

Biochemical and Biophysical Research Communications

Volumn 315, Issue 3, 2004, Pages 739-745

  Kishimoto, Aiko ^a,b   Hasegawa, Kazuya ^c,d   Suzuki, Hirofumi ^c   Taguchi, Hideki ^a   Namba, Keiichi ^b,c   Yoshida, Masasuke ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d JAPAN SYNCHROTRON RADIATION RESEARCH INSTITUTE   (Japan)

Author keywords

Amyloid; Cross ; Fiber; Nanotube; Prion; Sup35; X ray diffraction; Helix

Indexed keywords

AMYLOID; NANOTUBE; PRION PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CONTROLLED STUDY; HYDRATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; X RAY DIFFRACTION; YEAST;

EID: 1242340413     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.117     Document Type: Article

References (39)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
2. Horwich A.L., Weissman J.S. Deadly conformations-protein misfolding in prion disease. Cell. 89:1997;499-510.
3. Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 264:1994;566-569.
4. Zhou P., Derkatch I.L., Uptain S.M., Patino M.M., Lindquist S., Liebman S.W. The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3. EMBO J. 18:1999;1182-1191.
5. Sondheimer N., Lindquist S.L. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell. 5:2000;163-172.
6. 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.
7. Osherovich L.Z., Weissman J.S. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)]. Cell. 106:2001;183-194.
8. Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:1998;101-106.
9. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
10. Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24:1999;58-63.
11. Inouye H., Fraser P.E., Kirschner D.A. Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by X-ray diffraction. Biophys. J. 64:1993;502-519.
12. Kuwata K., Matsumoto T., Cheng H., Nagayama K., James T.L., Roder H. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. USA. 100:2003;14790-14795.
13. Balbirnie M., Grothe R., Eisenberg D.S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA. 98:2001;2375-2380.
14. Diaz-Avalos R., Long C., Fontano E., Balbirnie M., Grothe R., Eisenberg D., Caspar D.L. Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide. J. Mol. Biol. 330:2003;1165-1175.
15. Petkova A.T., Buntkowsky G., Dyda F., Leapman R.D., Yau W.M., Tycko R. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J. Mol. Biol. 335:2004;247-260.
16. Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science. 268:1995;880-884.
17. Patino M.M., Liu J.J., Glover J.R., Lindquist S.L. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science. 273:1996;622-626.
18. Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., Lindquist S.L. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 89:1997;811-819.
19. Paushkin S.V., Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D. In vitro propagation of the prion-like state of yeast Sup35 protein. Science. 277:1997;381-383.
20. DePace A.H., Santoso A., Hillner P., Weissman J.S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell. 93:1998;1241-1252.
21. parrer H.E., Santoso A.M., Szoka F.C. Jr., Weissman J.S. Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein. Science. 289:2000;595-599.
22. Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., Arnsdorf M.F., Lindquist S.L. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science. 289:2000;1317-1321.
23. Scheibel T., Kowal A.S., Bloom J.D., Lindquist S.L. Bidirectional amyloid fiber growth for a yeast prion determinant. Curr. Biol. 11:2001;366-369.
24. Ter-Avanesyan M.D., Dagkesamanskaya A.R., Kushnirov V.V., Smirnov V.N. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics. 137:1994;671-676.
25. Liu J.J., Sondheimer N., Lindquist S.L. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc. Natl. Acad. Sci. USA. 99:2002;16446-16453.
26. Inoue Y., Kishimoto A., Hirao J., Yoshida M., Taguchi H. Strong growth polarity of yeast prion fiber revealed by single fiber imaging. J. Biol.Chem. 276:2001;35227-35230.
27. 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.
28. 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.
29. 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.
30. Perutz M.F., Finch J.T., Lesk A. Amyloid fibers are water-filled nanotubes. Proc. Natl. Acad. Sci. USA. 99:2002;5591-5595.
31. Yamashita I., Vonderviszt F., Noguchi T., Namba K. Preparing well-oriented sols of straight bacterial flagellar filaments for X-ray fiber diffraction. J. Mol. Biol. 217:1991;293-302.
32. Yamashita I., Suzuki H., Namba K. Multiple-step method for making exceptionally well-oriented liquid-crystalline sols of macromolecular assemblies. J. Mol. Biol. 278:1998;609-615.
33. Serpell L.C., Berriman J., Jakes R., Goedert M., Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. USA. 97:2000;4897-4902.
34. Wetzel R. Ideas of order for amyloid fibril structure. Structure. 10:2002;1031-1036.
35. Pickersgill R.W. A primordial structure underlying amyloid. Structure. 11:2003;137-138.
36. 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.
37. Petkova A.T., Ishii Y., Balbach J.J., Antzutkin O.N., Leapman R.D., Delaglio F., Tycko R. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. USA. 99:2002;16742-16747.
38. Kraulis P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:1991;946-950.
39. Merritt E.A., Bacon D.J. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.