Conservation of the prion properties of Ure2p through evolution

Molecular Biology of the Cell

Volumn 14, Issue 8, 2003, Pages 3449-3458

  Baudin Baillieu, Agnès ^b   Fernandez Bellot, Eric ^c   Reine, Fabienne ^b   Coissac, Eric ^d   Cullin, Christophe ^a  

^a Institut de Biochimie et Genetique Cellulaires   (France)

^b CENTRE DE GÉNÉTIQUE MOLÉCULAIRE   (France)

^c UNIVERSITY OF KENT   (United Kingdom)

^d INSTITUT JACQUES MONOD   (France)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEIN URE2P; UNCLASSIFIED DRUG;

ARTICLE; CANDIDA ALBICANS; COMPUTER ANALYSIS; EVOLUTION; FUNGAL STRAIN; GENE DELETION; GENE INDUCTION; GENE ISOLATION; GENE SEQUENCE; KLUYVEROMYCES; NONHUMAN; NUCLEOTIDE SEQUENCE; PRION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; SACCHAROMYCES PARADOXUS; SACCHAROMYCES UVARUM; SCHIZOSACCHAROMYCES POMBE; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; EVOLUTION, MOLECULAR; MOLECULAR SEQUENCE DATA; PRIONS; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ANALYSIS; YEASTS;

CANDIDA; CANDIDA ALBICANS; KLUYVEROMYCES; KLUYVEROMYCES LACTIS; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES PARADOXUS; SACCHAROMYCES UVARUM; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE;

EID: 0041968890     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-01-0007     Document Type: Article

References (35)

1. Aigle, M., and Lacroute, F. (1975). Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol. Gen. Genet. 136, 327-335.
2. Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D.J. (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402.
3. Bousset, L., Belrhali, H., Janin, J., Melki, R., and Morera, S. (2001). Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9, 39-46.
4. Bucciantini, M. et al. (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511.
5. Chernoff, Y.O., Lindquist, S.L., Ono, B., Inge, V.S., and Liebman, S.W. (1995). Role of the chaperone protein Hspl04 in propagation of the yeast prion-like factor [psi+]. Science 268, 880-884.
6. Cullin, C., and Minvielle, S.L. (1994). Multipurpose vectors designed for the fast generation of N- or C- terminal epitope-tagged proteins. Yeast 10, 105-112.
7. Derkatch, I.L., Bradley, M.E., Hong, J.Y., and Liebman, S.W. (2001). Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106, 171-182.
8. Derkatch, I.L., Bradley, M.E., Masse, S.V., Zadorsky, S.P., Polozkov, G.V., Inge-Vechtomov, S.G., and Liebman, S.W. (2000). Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast? EMBO J. 19, 1942-1952.
9. Derkatch, I.L., Bradley, M.E., Zhou, P., Chernoff, Y.O., and Liebman, S.W. (1997). Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147, 507-519.
10. Derkatch, I.L., Chernoff, Y.O., Kushnirov, V.V., Inge, V.S., and Liebman, S.W. (1996). Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144, 1375-1386.
11. 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.
12. Edskes, H.K., Gray, V.T., and Wickner, R.B. (1999). The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. USA 96, 1498-1503.
13. Edskes, H.K., and Wickner, R.B. (2002). Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc. Natl. Acad. Sci. USA 99(Suppl 4), 16384-16391.
14. Feldmann, H. (2000). Genolevures - a novel approach to 'evolutionary genomics.' FEBS Lett. 487, 1-2.
15. Fernandez-Bellot, E., Guillemet, E., Baudin-Baillieu, A., Gaumer, S., Komar, A.A., and Cullin, C. (1999). Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. Biochem. J. 338, 403-407.
16. Fernandez-Bellot, E., Guillemet, E., and Cullin, C. (2000). The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J. 19, 3215-3222.
17. Gietz, D.G., St. Jean, A., Woods, R.A., and Schiestl, R.H. (1992). Improved method for hight***** efficiency transformation of intact cells. Nucleic Acids Res. 20, 142.
18. Kochneva-Pervukhova, N.V., Paushkin, S.V., Kushnirov, V.V., Cox, B.S., Tuite, M.F., and Ter-Avanesyan, M.D. (1998). Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein. EMBO J. 17, 5805-5810.
19. Kretzschmar, H.A., Stowring, L.E., Westaway, D., Stubblebine, W.H., Prusiner, S.B., and Dearmond, S.J. (1986). Molecular cloning of a human prion protein cDNA. DNA 5, 315-324.
20. Kushnirov, V.V., Kochneva-Pervukhova, N.V., Chechenova, M.B., Frolova, N.S., and Ter-Avanesyan, M.D. (2000). Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J. 19, 324-331.
21. Kushnirov, V.V., Ter, A.M., Telckov, M.V., Surguchov, A.P., Smirnov, V.N., and Inge, V.S. (1988). Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae. Gene 66, 45-54.
22. Lacroute, F. (1971). Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106, 519-522.
23. Maddelein, M.L., and Wickner, R.B. (1999). Two prion-inducing regions of Ure2p are nonoverlapping. Mol. Cell. Biol. 19, 4516-4524.
24. Masison, D., and Wickner, R.B. (1995). Prion-inducing domain of yeast ure2p and protease resistance of ure2p in prion-containing cells. Science 270, 93-95.
25. Michelitsch, M.D., and Weissman, J.S. (2000). A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 97, 11910-11915.
26. Moriyama, H., Edskes, H.K., and Wickner, R.B. (2000). [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20, 8916-8922.
27. Nakayashiki, T., Ebihara, K., Bannai, H., and Nakamura, Y. (2001). Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol. Cell 7, 1121-1130.
28. Osherovich, L.Z., and Weissman, J.S. (2001). Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 106, 183-194.
29. Resende, C., Parham, S.N., Tinsley, C., Ferreira, P., Duarte, J.A., and Tuite, M.F. (2002). The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism. Microbiology 148, 1049-1060.
30. Santoso, A., Chien, P., Osherovich, L.Z., and Weissman, J.S. (2000). Molecular basis of a yeast prion species barrier. Cell 100, 277-288.
31. Sondheimer, N., and Lindquist, S. (2000). Rnq 1, an epigenetic modifier of protein function in yeast. Mol. Cell 5, 163-172.
32. Ter-Avanesyan, M.D., Dagkesamanskaya, A.R., Kushnirov, V.V., and Smirnov, V.N. (1994). The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 137, 671-676.
33. Thual, C., Komar, A.A., Bousset, L., Fernandez-Bellot, E., Cullin, C., and Melki, R. (1999). Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J. Biol. Chem. 274, 13666-13674.
34. Umland, T.C., Taylor, K.L., Rhee, S., Wickner, R.B., and Davies, D.R. (2001). The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA 98, 1459-1464.
35. Wickner, R.B. (1994). [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569.