Prion stability

Protein-Based Inheritance

Volumn , Issue , 2007, Pages 56-72

  Cox, Brian S ^a   Byrne, Lee ^a   Tuite, Mick F ^a  

^a UNIVERSITY OF KENT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 70449640074     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781498712507-11     Document Type: Chapter

References (58)

1. Coustou V, Deleu C, Saupe S et al. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci USA 1997; 94:9773-9778.
2. Wickner RB. [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264:566-569.
3. Cox BS. Prion-like factors in yeast. Curr Biol 1994; 4:744-748.
4. +]. Cell 2001; 106:171-182.
5. +] prion. Oil 2001; 106:183-194.
6. Tanaka M, Collins SR, Toyama BH et al. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585-589.
7. +] prion in yeast. Genetics 2003; 165:23-33.
8. Lund PM, Cox BS. Reversion analysis of [psi"] mutants in Saccharomyces cerevisiae. Genet Res 1981; 37:173-182.
9. Juliani MH, Gambarini AG, Da Costa MOP. Induction of rho-minus mutants in Saccharomyces cerevisiae by guanidine hydrochloride. I. enedc analysis. Mutation Res 1975; 29:67-75.
10. Derkach IL, Bradley ME, Zhou P et al. Genetic and environmental factors affecting the de novo appearance of the [PST] prion in Saccharomyces cerevisiae. Genetics 1997; 147:507-519.
11. Masison DC, Maddelein ML, Wickner RB. The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation. Proc Natl Acad Sci USA 1997; 94:12503-12508.
12. Bradley ME, Edskes HK, Hong JY et al. Interactions among prions and prion “strains” in yeast. Proc Natl Acad Sci USA 2002; 99(suppl. 4):16392-16399.
13. Chernoff YO, Derkach IL, Inge-Vechtomov SG. Multicopy SUP35 gene induces the dc novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 1993; 24:268-270.
14. Sondheimer N, Lindquist S. Rnql: An epigenetic modifier of protein function in yeast. Molec Cell 2000; 5:163-172.
15. Derkach IL, Chernoff YO, Kushnirov W et al. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 1996; 144:1375-1386.
16. Masison DC, Wickner RB. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2’ in prion-containing cells. Science 1995; 270:93-95.
17. Roberts BT, Wickner RB. A new kind of prion. Cell Cycle 2004; 3:100-103
18. +]: A two-prion system in yeast? EMBO J 2000; 19:1942-1952.
19. +] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci USA 2004; 101:12934-12939.
20. Salnikova AB, Kryndushkin DS, Smirnov VN et al. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its nonheritable amyloids. J Biol Chem 2005; 280:8808-8812.
21. +] determinant in Saccharomyces cerevisiae. Curr Genet 1998; 34:146-151.
22. Fernandez-Bellot E, Guillemet E, Cullin C. The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J 2000; 19:3215-3222.
23. Hatin I, Bidou L, Cullin C et al. Translational errors as an early event in prion conversion. Cell Mol Biol (Noisy-le-grand) 2001; 47:23-28, (Online Pub. OL).
24. Kolotova-Levine N, Merritt G, Tuite MF. Unpublished results.
25. Liu JJ, Lindquist S. Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast. Nature 1999; 400:573-576.
26. Parham SN, Resende CG, Tuite MF. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J 2001; 20:2111-2119.
27. De Pace AH, Santoso A, Hillner P et al. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Nature Struct Biol 2002; 9:389-396.
28. Santoso A, Chien P, Osherovich LZ et al. Molecular basis of a yeast prion species barrier. Cell 2000; 100:277-288.
29. Osherovich LZ, Cox BS, Tuite MF et al. Dissection and design of yeast prions. PLoS Biology 2004; 2:0442.
30. +], a novel Sup35-prion variant propagated with non-Glu/Asn oligopeptide repeats in the absence of the chaperone protein, Hsp104. Genes and Cells 2003; 8:603-618.
31. Tanaka M, Chien P, Naber N et al. Conformational variations in an infectious protein determine prion strain differences. Nature 2004; 428:265-267.
32. King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004; 428:319-323.
33. Satpute-Krishnan P, Serio TR. Prion protein remodelling confers an immediate phenotypic switch. Nature 2005; 437:262-265.
34. Mehta S, Yang XM, Chan CS et al. The 2-micron plasmid purloins the yeast cohesin complex: A mechanism for coupling plasmid partitioning and chromosome segregation. J Cell Biol 2002; 158:625-637.
35. +]. Science 1995; 268:880-884.
36. Tuite MF. D. Phil Thesis. Oxford: 1979.
37. −] in Saccharomyces cerevisiae. Genetics 1981; 98:691-711.
38. Glover JR, Lindquist SL. Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 1998; 94:73-82.
39. +] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol 2001; 40:1357-1369.
40. Jung G, Masison DC. Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions. Curr Microbiol 2001; 43:7-10.
41. +] of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 2000; 97:240-244.
42. Ness F, Ferreira P, Cox BS et al. Guanidine hydrochloride inhibits the generation of prion seeds but not prion protein aggregation in yeast. Mol Cell Biol 2002; 22:5593-5605
43. Cole DJ, Morgan BJT, Ridout MS et al. Estimating the number of prions in yeast cells. Mathematical Medicine and Biology 2004; 21:369-395.
44. Cox BS. In: Hall MD, Linder P, eds. Psi Phenomena in Yeast: Early Days of Yeast Genetics. NY: Cold Spring Harbor Laboratory Press, 1993:477.
45. Kushnirov W, Ter-Avenasyan MD. Structure and replication of yeast prions. Cell 1998; 94:13-16.
46. Wegrzyn RD, Bapat K, Newnam GP et al. Mechanisms of prion loss after Hsp104 inactivation in yeast. Molec Cell Biol 2001; 21:4656-4669.
47. Ripaud L, Maillet L, Cullin C. The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products. EMBO J 2003; 22:5251-5259.
48. Singh A, Helms C, Sherman F. Mutation of the non-Mendelian suppressor, Psi, in yeast by hypertonic media. Proc Natl Acad Sci USA 1979; 76:1952-1956.
49. Tuite MF, Cox BS. Ultraviolet mutagenesis studies of [psi], a cytoplasmic determinant of Saccharomyces cerevisae. Genetics 1980; 95:611-630.
50. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 2003; 278:49636-49643.
51. Liebman SL, Derkach IL. Prion-Prion interactions. 2007; this volume.
52. +] prion in yeast. 2007; this volume.
53. Rikhvanov EG, Romanova NV, Chernoff YO. Chaperone effects on prion and nonprion aggregates. 2007; this volume.
54. +] prion by guanidine inactivation of Hsp104 does not require cell division. Proc Natl Acad Sci USA 2005; 102:12789-12794.
55. Borchsenius AS, Wegrzyn RD, Newnam GP et al. Yeast prion protein derivative defective in aggregate shearing and production of new ‘seeds’. EMBO J 2001; 20:6683-6691.
56. Futcher AB. The 2 micron circle plasmid of Saccharomyces cerevisiae. Yeast 1988; 4:27-40.
57. +], a prion-like form of release factor eRF3. EMBO J 1999; 18:1182-1191.
58. Borchsenius AS, Muller S, Newnam GP et al. Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet 2006; 49:21-29.