[PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104

Genes to Cells

Volumn 8, Issue 7, 2003, Pages 603-618

  Crist, Colin G ^a   Nakayashiki, Toru ^a   Kurahashi, Hiroshi ^a   Nakamura, Yoshikazu ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; ASPARAGINE; CHAPERONE; GLUTAMIC ACID; HEAT SHOCK PROTEIN 104; OLIGOPEPTIDE; PRION PROTEIN; REGULATOR PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BUDDING; CONTROLLED STUDY; CYTOPLASM; DNA RESPONSIVE ELEMENT; ELIMINATION REACTION; FREQUENCY ANALYSIS; FUNGAL STRAIN; GENE INACTIVATION; GENE REPLICATION; GENETIC STABILITY; GENETIC VARIABILITY; IN VITRO STUDY; INHERITANCE; MAMMAL; MOLECULAR SIZE; NONHUMAN; NUCLEOTIDE REPEAT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN TRANSPORT; RNA TRANSLATION; YEAST;

AMINO ACID SEQUENCE; ASPARAGINE; BASE SEQUENCE; DNA PRIMERS; GLYCINE; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; PRIONS; REPETITIVE SEQUENCES, AMINO ACID; SACCHAROMYCES CEREVISIAE PROTEINS;

MAMMALIA; MAMMALIAN PRIONS; SACCHAROMYCETALES;

EID: 0038714894     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2443.2003.00661.x     Document Type: Article

References (45)

1. Borchsenius, A.S., Wegrzyn, R.D., Newnam, G.P., Inge-Vechtomov, S.G. & Chernoff, Y.O. (2001) Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J. 20, 6683-6691.
2. +]. Science 268, 880-884.
3. Chiesa, R., Piccardo, P., Ghetti, B. & Harris, D.A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351.
4. Collinson, S.K., Parker, J.M., Hodges, R.S. & Kay, W.W. (1999) Structural predictions of AgfA, the insoluble fimbrial subunit of Salmonella thin aggregative fimbriae. J. Mol. Biol. 290, 741-756.
5. Cox, B.S. (1965) Ψ, a cytoplasmic suppressor of super-suppressor in yeast, Heredity 20, 505-521.
6. DePace, A.H., Santoso, A., Hillner, P. & Weissman, J.S. (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241-1252.
7. +]. Cell 106, 171-182.
8. +] of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97, 240-244.
9. +] prion by guanidine hyrdrochloride is the result of Hsp104 inactivation. Mol. Microbiol. 40, 1357-1369.
10. Flechsig, E., Shmerling, D., Hegyi, I., et al. (2000) Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 27, 399-408.
11. Glover, J.R. & Lindquist, S. (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82.
12. Goedert, M., Spillantini, M.G. & Davies, S.W. (1998) Filamentous nerve cell inclusions in neurodegenerative diseases. Curr. Opin. Neurobiol. 8, 619-632.
13. Gottesman, S., Wickner, S. & Maurizi, M.R. (1997) Protein quality control: triage by chaperones and proteases. General Dev. 11, 815-823.
14. Ivanov, P.A., Lewitin, E.I., Shevelev, B.I., et al. (2001) Sup35p yeast prion-like protein as an adapter for production of the Gag-p55 antigen of HIV-1 and the 1-chain of botulinum neurotoxin in Saccharomyces cerevisiae. Res. Microbiol. 152, 27-35.
15. Jung, G., Jones, G. & Masison, D.C. (2002) Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc. Natl. Acad. Sci. USA 99, 9936-9941.
16. Jung, G. & Masison, D.C. (2001) Guanidine hydrochloride inhibits hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol. 43, 7-10.
17. Kajava, A.V., Cheng, N., Cleaver, R., et al. (2001) Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. Mol. Microbiol. 42, 279-292.
18. Klunk, W.E., Pettegrew,J.W. & Abraham, D.J. (1989) Two simple methods for quantitating low-affinity dye-substrate binding. J. Histochem. Cytochem. 37, 1293-1297.
19. Kretzschmar, H.A., Stowring, L.E., Westaway, D., Stubblebine, W.H., Prusiner, S.B. & Dearmond, S.J. (1986) Molecular cloning of a human prion protein cDNA. DNA 5, 315-324.
20. Kushnirov, V.V. & Ter-Avanesyan, M.D. (1998) Structure and replication. of yeast prions. Cell 94, 13-16.
21. Kushnirov, V.V., Ter-Avanesyan, M.D., Telckov, M.V., Surguchov, A.P., Smirnov, V.N. & Inge-Vechtomov, S.G. (1988) Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae. Gene 66, 45-54.
22. Li, L. & Lindquist, S. (2000) Creating a protein-based element of inheritance. Science 287, 661-664.
23. Lindquist, S. (1997) Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89, 495-498.
24. Liu, J.J. & Lindquist, S. (1999) Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400, 573-576.
25. +]. Proc. Natl. Acad. Sci. USA 99, 16446-16453.
26. Masison, D.C. & Wickner, R.B. (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270, 93-95.
27. Nakamura, Y., Ito, K. & Ehrenberg, M. (2000) Mimicry grasps reality in translation termination. Cell 101, 349-352.
28. +] 'prions' that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol. Cell 7, 1121-1130.
29. Ness, F., Ferreira, P., Cox, B.S. & Tuite, M.F. (2002) Guanidine hydrochloride inhibits the generation of prion 'seeds' but not prion protein aggregation in yeast. Mol. Cell. Biol. 22, 5593-5605.
30. Orr, H.T. (2001) Beyond the Qs in the polyglutamine diseases. General Dev. 15, 925-932.
31. Parham, S.N., Resende, C.G. & Tuite, M.F. (2001) Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20, 2111-2119.
32. Patino, M.M., Liu, J.J., Glover, J.R. & Lindquist, S. (1996) Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
33. +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134.
34. Prusiner, S.B. & Scott, M.R. (1997) Genetics of prions. Annu. Rev. Genet. 31, 139-175.
35. Rose, M.D. & Fink, G.R. (1987) KAR1, a gene required for function of both intranuclear and extranuclear microtubules in yeast. Cell 48, 1047-1060.
36. Santoso, A., Chien, P., Osherovich, L.Z. & Weissman, J.S. (2000) Molecular basis of a yeast prion species barrier. Cell 100, 277-288.
37. Schirmer, E.C. & Lindquist, S. (1997) Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Proc. Natl. Acad. Sci. USA 94, 13932-13937.
38. Serio, T.R., Cashikar, A.G., Kowal, A.S., et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317-1321.
39. Sikorski, R.S. & Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
40. Stansfield, I., Jones, K.M., Kushnirov, V.V., et al. (1995) The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365-4373.
41. +] in the yeast Saccharomyces cerevisiae. Genetics 137, 671-676.
42. Ter-Avanesyan, M.D., Kushnirov, V.V., Dagkesamanskaya, A.R., et al. (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.
43. Volkov, K.V., Aksenova, A.Y., Soom, M.J., et al. (2002) Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae. Genetics 160, 25-36.
44. Wegrzyn, R.D., Bapat, K., Newnam, G.P., Zink, A.D. & Chernoff, Y.O. (2001) Mechanism of prion loss after hsp104 inactivation in yeast. Mol. Cell. Biol. 21, 4656-4669.
45. Zhouravleva, G., Frolova, L., Le Goff, X., et al. (1995) Terminadon of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065-4072.