A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion

Cell

Volumn 93, Issue 7, 1998, Pages 1241-1252

  DePace, Angela H ^a   Santoso, Alex ^a   Hillner, Paul ^a   Weissman, Jonathan S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLUTAMINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; GENE MUTATION; NONHUMAN; PLASMID; PRION; PRIORITY JOURNAL; PROTEIN EXPRESSION; YEAST;

EID: 0032568793     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81467-1     Document Type: Article

References (38)

1. Ausubel, F.M., Brent, R., Kingston, R.C., Moore, R.D., Seidman, J.G., Smith, J.A., and Struhl, K. (1995). Current Protocols in Molecular Biology (New York: John Wiley and Sons, Inc.).
2. Briehl, R.W. (1980). Solid-like behaviour of unsheared sickle haemoglobin gels and the effects of shear. Nature 288, 622-624.
3. Caughey, B., and Chesebro, B. (1997). Prion protein and the transmissible spongiform encephalopathies. Trends Cell. Biol. 7, 56-62.
4. Chernoff, Y.O., Lindquist, S.L., Ono, B., Inge-Vechtomov, S.G., and Liebman, S.W. (1995). Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268, 880-884.
5. Christianson, T.W., Sikorski, R.S., Dante, M., Shero, J.H., and Hieter, P. (1992). Multifunctional yeast high-copy-number shuttle vectors. Gene 110, 119-122.
6. Cox, B.S., Tuite, M.P., and McLaughlin, C.S. (1988). The psi factor of yeast: a problem in inheritance. Yeast 4, 159-178.
7. Doel, S.M., McCready, S.J., Nierras, C.R., and Cox, B.S. (1994). The dominant PNM2-mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137, 659-670.
8. Glover, J., Kowal, A., Schirmer, E., Patino, M., Liu, J., and Lindquist, S. (1997). Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89, 811-819.
9. Harper, J.D., and Lansbury, P.T., Jr. (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66, 385-407.
10. Harper, J.D., Wong, S.S., Lieber, C.M., and Lansbury, P.T. (1997a). Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
11. Harper, J.D., Lieber, C.M., and Lansbury, P.T., Jr. (1997b). Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem. Biol. 4, 951-959.
12. Jaenicke, R., and Seckler, R. (1997). Protein misassembly in vitro. Adv. Protein Chem. 50, 1-59.
13. Jahlem, P., Green, H., and Djian, P. (1998). Transglutaminase action imitates Huntingtin's disease: selective polymerization of Huntingtin containing expanded polyglutamine. Mol. Cell 1, 595-601.
14. Jarrett, J.T., and Lansbury, P.T.J. (1993). Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
15. Kaneko, K., Zulianello, L., Scott, M., Cooper, C.M., Wallace, A.C., James, T.L., Cohen, F.E., and Prusiner, S.B. (1997). Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94, 10069-10074.
16. Kelly, J.W., Colon, W., Lai, Z., Lashuel, H.A., McCulloch, J., McCutchen, S.L., Miroy, G.J., and Peterson, S.A. (1997). Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Protein Chem. 50, 161-181.
17. King, C.Y., Tittmann, P., Gross, H., Gebert, R., Aebi, M., and Wüthrich, 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.
18. Klunk, W.E., Pettegrew, J.W., and Abraham, D.J. (1989). Two simple methods for quantitating low-affinity dye-substrate binding. J. Histochem. Cytochem. 37, 1293-1297.
19. Kushnirov, V., Ter-Avanesyan, M., Didichenko, S., Smirnov, V., Chernoff, Y., Derkach, I., Novikova, O., Inge-Vechtomov, S., Neistat, M., and Tolstorukov, I. (1990). Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae. Yeast 6, 461-472.
20. Lansbury, P.T., Jr., Costa, P.R., Griffiths, J.M., Simon, E.J., Auger, M., Halverson, K.J., Kocisko, D.A., Hendsch, Z.S., Ashburn, T.T., Spencer, R.G., et al. (1995). Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2, 990-998.
21. Lazo, N.D., and Downing, D.T. (1998). Amyloid fibrils may be assembled from beta-helical protofibrils. Biochemistry 37, 1731-1735.
22. Lindquist, S. (1997). Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89, 495-498.
23. Liu, Y., Hart, P.J., Schlunegger, M.P., and Eisenberg, D. (1998). The crystal structure of a 3D domain-swapped dimer of RNaseA at 2.1Å resolution. Proc. Natl. Acad. Sci. USA 95, 3437-3442.
24. Patino, M., Liu, J., Glover, J., and Lindquist, S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
25. Paulson, H.L., Perez, M.K., Trottier, Y., Trojanowski, J.Q., Subramony, S.H., Das, S.S., Vig, P., Mandel, J.-L., Fischbeck, K.H., and Pittman, R.N. (1997). Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19, 333-344.
26. Paushkin, S.V., Kushnirov, V.V., Smirnov, V.N., and Ter-Avanesyan, M.D. (1996). Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134.
27. Paushkin, S., Kushnirov, V., Smirnov, V., and Ter-Avanesyan, M. (1997). In vitro propagation of the prion-like state of yeast Sup35 protein. Science 277, 381-383.
28. Prusiner, S.B., Scott, M.R., DeArmond, S.J., and Cohen, F.E. (1998). Prion protein biology. Cell 93, 337-348.
29. Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G.P., Davies, S.W., Lehrach, H., and Wanker, E.E. (1997). Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90, 549-558.
30. Sherman, F, (1991). Getting started with yeast. Meth. Enzymol. 194, 3-21.
31. Stansfield, I., Jones, K.M., Kushnirov, V.V., Dagkesamanskaya, A.R., Poznyakovski, A.I., Paushkin, S.V., Nierras, C.R., Cox, B.S., Ter-Avanesyan, M.D., and Tuite, M.F. (1995). The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365-4373.
32. Stott, K., Blackburn, J., Butler, P., and Perutz, M. (1995). Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases. Proc. Natl. Acad. Sci. USA 92, 6509-6513.
33. Sunde, M., and Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50, 123-159.
34. Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., and Blake, C.C.F. (1997). Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739.
35. Ter-Avanesyan, M., Kushnirov, V., Dagkesamanskaya, A., Didichenko, S., Chernoff, Y., Inge-Vechtomov, S., and Smirnov, V. (1993). Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683-692.
36. Wetzel, R. (1997). Domain stability in immunoglobulin light chain deposition disorders. Adv. Protein Chem. 50, 183-242.
37. Wickner, R.B. (1994). [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569.
38. Wickner, R.B., Masison, D.C., and Edskes, H.K. (1995). [PSI] and [URE3] as yeast prions. Yeast 11, 1671-1685.