Mutants of the pafl complex alter phenotypic expression of the yeast prion [PSI+]

Molecular Biology of the Cell

Volumn 20, Issue 8, 2009, Pages 2229-2241

  Strawn, Lisa A ^a   Lin, Changyi A ^a   Tank, Elizabeth M H ^a   Osman, Morwan M ^a   Simpson, Sarah A ^a   True, Heather L ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PAF1 PROTEIN; PRION PROTEIN; TRANSCRIPTION FACTOR; TRANSLATION TERMINATION FACTOR; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; CTR9 PROTEIN, S CEREVISIAE; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; PAF1 PROTEIN, S CEREVISIAE; RTF1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TATA BINDING PROTEIN; TRANSCRIPTION ELONGATION FACTOR;

ARTICLE; CELL SURVIVAL; COMPLEX FORMATION; DNA MODIFICATION; EPIGENETICS; EUKARYOTE; GENE DELETION; GENE MUTATION; GENETIC VARIABILITY; MUTANT; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; REGULATORY MECHANISM; RNA TRANSLATION; STOP CODON; TRANSCRIPTION REGULATION; YEAST; ALLELE; CHEMISTRY; CYTOLOGY; GENE EXPRESSION REGULATION; GENE REPRESSION; GENETIC COMPLEMENTATION; GENETICS; METABOLISM; MUTATION; PRION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SYNTHESIS; RECESSIVE GENE; RNA PROCESSING; SACCHAROMYCES CEREVISIAE;

EUKARYOTA;

ALLELES; CELL CYCLE PROTEINS; CODON, NONSENSE; GENE DELETION; GENE EXPRESSION REGULATION, FUNGAL; GENES, RECESSIVE; GENETIC COMPLEMENTATION TEST; MULTIPROTEIN COMPLEXES; MUTATION; NUCLEAR PROTEINS; PHENOTYPE; PRIONS; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, QUATERNARY; RNA PROCESSING, POST-TRANSCRIPTIONAL; RNA, MESSENGER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUPPRESSION, GENETIC; TATA-BOX BINDING PROTEIN; TRANSCRIPTIONAL ELONGATION FACTORS;

EID: 65249116416     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-08-0813     Document Type: Article

References (98)

1. Bagriantsev, S., and Liebman, S. W. (2004). Specificity of prion assembly in vivo. [PSI + ] and [PIN+] form separate structures in yeast. J. Biol. Chem. 279, 51042-51048.
2. Baudin, A., Ozier-Kalogeropoulos, O., Denouel, A., Lacroute, F., and Cullin, C. (1993). A simple and efficient method for direct gene deletion in Saccharo-myces cerevisiae. Nucleic Acids Res. 21, 3329-3330.
3. Beier, H., and Grimm, M. (2001). Misreading of termination codons in eu-karyotes by natural nonsense suppressor tRNAs. Nucleic Acids Res. 29, 4767-4782.
4. Beilharz, T. H., and Preiss, T. (2007). Widespread use of poly(A) tail length control to accentuate expression of the yeast transcriptome. RNA 13, 982-997.
5. Bertram, G., Innes, S., Minella, O., Richardson, J., and Stansfield, I. (2001). Endless possibilities: translation termination and stop codon recognition. Microbiology 147, 255-269.
6. Betz, J. L., Chang, M., Washburn, T. M., Porter, S. E., Mueller, C. L., and Jaehning, J. A. (2002). Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol. Genet. Genomics 268, 272-285.
7. Bousse, T., Matrosovich, T., Portner, A., Kato, A., Nagai, Y., and Takimoto, T. (2002). The long noncoding region of the human parainfluenza virus type 1 f gene contributes to the read-through transcription at the m-f gene junction. J. Virol. 76, 8244-8251.
8. Bradley, M. E., Bagriantsev, S., Vishveshwara, N., and Liebman, S. W. (2003). Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45. Yeast 20, 625-632.
9. 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.
10. Chernoff, Y. O., Uptain, S. M., and Lindquist, S. L. (2002). Analysis of prion factors in yeast. Methods Enzymol. 351, 499-538.
11. Chu, Y., Simic, R., Warner, M. H., Arndt, K. M., and Prelich, G. (2007). Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J. 26, 4646-4656.
12. Cosson, B., Couturier, A., Chabelskaya, S., Kiktev, D., Inge-Vechtomov, S., Philippe, M., and Zhouravleva, G. (2002). Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation. Mol. Cell. Biol. 22, 3301-3315.
13. Cox, B. (1965). [Psi], A cytoplasmic suppressor of super-suppressor in yeast. Heredity 20, 505-521.
14. Cox, B. S. (1977). Allosuppressors in yeast. Gen. Res. 30, 197-205.
15. Czaplinski, K., Majlesi, N., Banerjee, T., and Peltz, S. W. (2000). Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiency. Rna 6, 730-743.
16. Czaplinski, K., Ruiz-Echevarria, M. J., Paushkin, S. V., Han, X., Weng, Y., Perlick, H. A., Dietz,H. C.,Ter-Avanesyan, M. D.,and Peltz,S. W. (1998). The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 12, 1665-1677.
17. DePace, A. H., Santoso, A., Hillner, P., and 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.
18. Derkatch, I. L., Chernoff, Y. O., Kushnirov, V. V., Inge-Vechtomov, S. G., and Liebman, S. W. (1996). Genesis and variability of [PSI] prion factors in Sac-charomyces cerevisiae. Genetics 144, 1375-1386.
19. 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.
20. Eaglestone, S. S., Cox, B. S., and Tuite, M. F. (1999). Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18, 1974-1981.
21. Firoozan, M., Grant, C. M., Duarte, J. A., and Tuite, M. F. (1991). Quantitation of readthrough of termination codons in yeast using a novel gene fusion assay. Yeast 7, 173-183.
22. Frolova, L., et al. (1994). A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature 372, 701-703.
23. Giacomelli, M. G., Hancock, A. S., and Masel, J. (2007). The conversion of 3′ UTRs into coding regions. Mol. Biol. Evol. 24, 457-464.
24. Gross, T., Siepmann, A., Sturm, D., Windgassen, M., Scarcelli, J. J., Seedorf, M., Cole, C. N., and Krebber, H. (2007). The DEAD-box RNA helicase Dbp5 functions in translation termination. Science 315, 646-649.
25. Gueldener, U., Heinisch, J., Koehler, G. J., Voss, D., and Hegemann, J. H. (2002). A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res. 30, e23.
26. Harrison, P., Kumar, A., Lan, N., Echols, N., Snyder, M., and Gerstein, M. (2002). A small reservoir of disabled ORFs in the yeast genome and its implications for the dynamics of proteome evolution. J. Mol. Biol. 316, 409-419.
27. Hatin, I., Fabret, C., Namy, O., Decatur, W. A., and Rousset, J. P. (2007). Fine-tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome. Genetics 177, 1527-1537.
28. Kandl, K. A., Munshi, R., Ortiz, P. A., Andersen, G. R., Kinzy, T. G., and Adams, A. E. (2002). Identification of a role for actin in translational fidelity in yeast. Mol. Genet. Genomics 268, 10-18.
29. Keeling, K. M., Salas-Marco, J., Osherovich, L. Z., and Bedwell, D. M. (2006). Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol. Cell Biol. 26, 5237-5248.
30. Kobayashi, O., Suda, H., Ohtani, T., and Sone, H. (1996). Molecular cloning and analysis of the dominant flocculation gene FLO8 from Saccharomyces cerevisiae. Mol. Gen. Genet. 251, 707-715.
31. Kobayashi, O., Yoshimoto, H., and Sone, H. (1999). Analysis of the genes activated by the FLO8 gene in Saccharomyces cerevisiae. Curr. Genet. 36, 256-261.
32. Koch, C., Wollmann, P., Dahl, M., and Lottspeich, F. (1999). A role for Ctr9p and Paf1p in the regulation G1 cyclin expression in yeast. Nucleic Acids Res. 27, 2126-2134.
33. Kochneva-Pervukhova, N. V., Chechenova, M. B., Valouev, I. A., Kushnirov, V. V., Smirnov, V. N., and Ter-Avanesyan, M. D. (2001). [Psi(+)j prion generation in yeast: characterization of the 'strain' difference. Yeast 18, 489-497.
34. Kofuji, S., Sakuno, T., Takahashi, S., Araki, Y., Doi, Y., Hoshino, S., and Katada, T. (2006). The decapping enzyme Dcp1 participates in translation termination through its interaction with the release factor eRF3 in budding yeast. Biochem. Biophys. Res. Commun. 344, 547-553.
35. Krishnan, R., and Lindquist, S. L. (2005). Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772.
36. Krogan, N. J., et al. (2003a). The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell 11, 721-729.
37. Krogan, N. J., Kim, M., Ahn, S. H., Zhong, G., Kobor, M. S., Cagney, G., Emili, A., Shilatifard, A., Buratowski, S., and Greenblatt, J. F. (2002). RNA polymer-ase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol. Cell. Biol. 22, 6979-6992.
38. Krogan, N. J., et al. (2003b). Methylation ofhistone H3 bySet2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II. Mol. Cell. Biol. 23, 4207-4218.
39. Kryndushkin, D. S., Alexandrov, I. M., Ter-Avanesyan, M. D., and Kushnirov, V. V. (2003). Yeast [PSI + ] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278, 49636-49643.
40. Kwapisz, M., Smagowicz, W. J., Oficjalska, D., Hatin, I., Rousset, J. P., Zo-ladek, T., and Boguta, M. (2002). Up-regulation of tRNA biosynthesis affects translational readthrough in maf1-delta mutant of Saccharomyces cerevisiae. Curr. Genet. 42, 147-152.
41. Lawrence, C. W. (1991). Classical mutagenesis techniques. Methods Enzymol. 194, 273-281.
42. Li, L., and Lindquist, S. (2000). Creating a protein-based element of inheritance. Science 287, 661-664.
43. Liebman, S. W., and All-Robyn, J. A. (1984). A non-Mendelian factor, [eta + ], causes lethality of yeast omnipotent-suppressor strains. Curr. Genet. 8, 567-573.
44. Lindquist, S., Krobitsch, S., Li, L., and Sondheimer, N. (2001). Investigating protein conformation-based inheritance and disease in yeast. Philos. Trans. R. Soc. Lond B Biol. Sci. 356, 169-176.
45. Liu, H., Styles, C.A., and Fink, G.R. (1996). Saccharomyces cerevisiae S288C has a mutation in FLO8, a gene required for filamentous growth. Genetics 144, 967-978.
46. Masel, J. (2006). Cryptic genetic variation is enriched for potential adaptations. Genetics 172, 1985-1991.
47. Masel, J., and Bergman, A. (2003). The evolution of the evolvability properties of the yeast prion [PSI + ]. Evolution 57, 1498-1512.
48. Mozdy, A. D., Podell, E. R., and Cech, T. R. (2008). Multiple yeast genes, including Paf1 complex genes, affect telomere length via telomerase RNA abundance. Mol. Cell. Biol. 28, 4152-4161.
49. Mueller, C. L., and Jaehning, J. A. (2002). Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol. Cell. Biol. 22, 1971-1980.
50. Mueller, C. L., Porter, S. E., Hoffman, M. G., and Jaehning, J. A. (2004). The Paf1 complex has functions independent of actively transcribing RNA poly-merase II. Mol. Cell 14, 447-456.
51. Muhlrad, D., and Parker, R. (1999). Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance. RNA 5, 1299-1307.
52. Nagalakshmi, U., Wang, Z., Waern, K., Shou, C., Raha, D., Gerstein, M., and Snyder, M. (2008). The transcriptional landscape of the yeast genome defined by RNA sequencing. Science 320, 1344-1349.
53. Namy, O., Duchateau-Nguyen, G., Hatin, I., Hermann-Le Denmat, S., Ter-mier, M., and Rousset, J. P. (2003). Identification of stop codon readthrough genes in Saccharomyces cerevisiae. Nucleic Acids Res. 31, 2289-2296.
54. Namy, O., Duchateau-Nguyen, G., and Rousset, J. P. (2002). Translational readthrough of the PDE2 stop codon modulates cAMP levels in Saccharomyces cerevisiae. Mol. Microbiol. 43, 641-652.
55. Namy, O., Galopier, A., Martini, C., Matsufuji, S., Fabret, C., and Rousset, J.P. (2008). Epigenetic control of polyamines by the prion [PSI(+)]. Nat. Cell Biol 10, 1069-1075.
56. Ng, H. H., Robert, F., Young, R. A., and Struhl, K. (2003). Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell 11, 709-719.
57. Nordick, K., Hoffman, M. G., Betz, J. L., and Jaehning, J. A. (2008). Direct interactions between the Paf1 complex and a cleavage and polyadenylation factor are revealed by dissociation of Paf1 from RNA polymerase II. Eukaryot. Cell 7, 1158-1167.
58. Patino, M. M., Liu, J. J., Glover, J. R., and Lindquist, S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
59. 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.
60. Penheiter, K. L., Washburn, T. M., Porter, S. E., Hoffman, M. G., and Jaehning, J. A. (2005). A posttranscriptional role for the yeast Paf1-RNA polymerase II complex is revealed by identification of primary targets. Mol. Cell 20, 213-223.
61. Poenisch, M., Wille, S., Staeheli, P., and Schneider, U. (2008). Polymerase read-through at the first transcription termination site contributes to regulation of Borna disease virus gene expression. J. Virol. 82, 9537-9545.
62. Pokholok, D. K., Hannett, N. M., and Young, R. A. (2002). Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol. Cell 9, 799-809.
63. Roberts, R. L., and Fink, G. R. (1994). Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: mating and invasive growth. Genes Dev. 8, 2974-2985.
64. Rondon, A. G., Gallardo, M., Garcia-Rubio, M., and Aguilera, A. (2004). Molecular evidence indicating that the yeast PAF complex is required for transcription elongation. EMBO Rep. 5, 47-53.
65. Rozenblatt-Rosen, O., Hughes, C. M., Nannepaga, S. J., Shanmugam, K. S., Copeland, T. D., Guszczynski, T., Resau, J. H., and Meyerson, M. (2005). The parafibromin tumor suppressor protein is part of a human Paf1 complex. Mol. Cell. Biol. 25, 612-620.
66. Schmitt, M. E., Brown, T. A., and Trumpower, B. L. (1990). A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18, 3091-3092.
67. Sheldon, K. E., Mauger, D. M., and Arndt, K. M. (2005). A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3′ end formation. Mol. Cell 20, 225-236.
68. Shi, X., Finkelstein, A., Wolf, A. J., Wade, P. A., Burton, Z. F., and Jaehning, J. A. (1996). Paf1p, an RNA polymerase II-associated factor in Saccharomyces cerevisiae, may have both positive and negative roles in transcription. Mol. Cell. Biol. 16, 669-676.
69. Sikorski, R. S., and 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.
70. Song, J. M., and Liebman, S. W. (1987). Allosuppressors that enhance the efficiency of omnipotent suppressors in Saccharomyces cerevisiae. Genetics 115, 451-460.
71. Squazzo, S. L., Costa, P. J., Lindstrom, D. L., Kumer, K. E., Simic, R., Jennings, J. L., Link, A. J., Arndt, K. M., and Hartzog, G. A. (2002). The Paf1 complex physically and functionally associates with transcription elongation factors in vivo. EMBO J. 21, 1764-1774.
72. Stansfield, I., Akhmaloka, and Tuite, M. F. (1995a). A mutant allele of the SUP45 (SAL4) gene of Saccharomyces cerevisiae shows temperature-dependent allosuppressor and omnipotent suppressor phenotypes. Curr. Genet. 27, 417-426.
73. 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. (1995b). The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365-4373.
74. Tanaka, M., Chien, P., Yonekura, K., and Weissman, J. S. (2005). Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121, 49-62.
75. Tank, E. M., Harris, D. A., Desai, A. A., and True, H. L. (2007). Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol. Cell. Biol. 27, 5445-5455.
76. Ter-Avanesyan, M. D., Dagkesamanskaya, A. R., Kushnirov, V. V., and Smir-nov, V. N. (1994). The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi + ] in the yeast Saccharo-myces cerevisiae. Genetics 137, 671-676.
77. Ter-Avanesyan, M. D., Kushnirov, V. V., Dagkesamanskaya, A. R., Didi-chenko, S. A., Chernoff, Y. O., Inge-Vechtomov, S. G., and Smirnov, V. N. (1993). Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevi-siae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683-692.
78. Toyama, B. H., Kelly, M. J., Gross, J. D., and Weissman, J. S. (2007). The structural basis of yeast prion strain variants. Nature 449, 233-237.
79. True, H. L., Berlin, I., and Lindquist, S. L. (2004). Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431, 184-187.
80. True, H. L., and Lindquist, S. L. (2000). A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477-483.
81. Tuite, M. F., Cox, B. S., and McLaughlin, C. S. (1983). In vitro nonsense suppression in [psi + ] and [psi-] cell-free lysates of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 80, 2824-2828.
82. Tuite, M. F., Mundy, C. R., and Cox, B. S. (1981). Agents that cause a high frequency of genetic change from [psi + ] to [psi - ]in Saccharomyces cerevisiae. Genetics 98, 691-711.
83. Uptain, S. M., Sawicki, G. J., Caughey, B., and Lindquist, S. (2001). Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J. 20, 6236-6245.
84. Urakov, V. N., Valouev, I. A., Lewitin, E. I., Paushkin, S. V., Kosorukov, V. S., Kushnirov, V. V., Smirnov, V. N., and Ter-Avanesyan, M. D. (2001). Itt1p, a novel protein inhibiting translation termination in Saccharomyces cerevisiae. BMC Mol. Biol. 2,9.
85. Valente, L., and Kinzy, T. G. (2003). Yeast as a sensor of factors affecting the accuracy of protein synthesis. Cell Mol. Life Sci. 60, 2115-2130.
86. Volkov, K., Osipov, K., Valouev, I., Inge-Vechtomov, S., and Mironova, L. (2007). N-terminal extension of Saccharomyces cerevisiae translation termination factor eRF3 influences the suppression efficiency of sup35 mutations. FEMS Yeast Res. 7, 357-365.
87. Volkov, K. V., Aksenova, A. Y., Soom, M. J., Osipov, K. V., Svitin, A. V., Kurischko, C., Shkundina, I. S., Ter-Avanesyan, M. D., Inge-Vechtomov, S. G., and Mironova, L. N. (2002). Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae. Genetics 160, 25-36.
88. von der Haar, T., and Tuite, M. F. (2007). Regulated translational bypass of stop codons in yeast. Trends Microbiol. 15, 78-86.
89. Wach, A., Brachat, A., Alberti-Segui, C., Rebischung, C., and Philippsen, P. (1997). Heterologous HIS3 marker and GFP reporter modules for PCR-target-ing in Saccharomyces cerevisiae. Yeast 13, 1065-1075.
90. Wach, A., Brachat, A., Pohlmann, R., and Philippsen, P. (1994). New heterol-ogous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-1808.
91. Wade, P. A., Werel, W., Fentzke, R. C., Thompson, N. E., Leykam, J. F., Burgess, R. R., Jaehning, J. A., and Burton, Z. F. (1996). A novel collection of accessory factors associated with yeast RNA polymerase II. Protein Expr. Purif. 8, 85-90.
92. Weng, Y., Czaplinski, K., and Peltz, S. W. (1996). Identification and characterization of mutations in the UPF1 gene that affect nonsense suppression and the formation of the Upf protein complex but not mRNA turnover. Mol. Cell. Biol. 16, 5491-5506.
93. Wickner, R. B., Masison, D. C., and Edskes, H. K. (1995). [PSI] and [URE3] as yeast prions. Yeast 11, 1671-1685.
94. Wilson, M. A., Meaux, S., Parker, R., and van Hoof, A. (2005). Genetic interactions between [PSI + ] and nonstop mRNA decay affect phenotypic variation. Proc. Natl. Acad. Sci. USA 102, 10244-10249.
95. Xiao, T., Kao, C. F., Krogan, N. J., Sun, Z. W., Greenblatt, J. F., Osley, M. A., and Strahl, B. D. (2005). Histone H2B ubiquitylation is associated with elongating RNA polymerase II. Mol. Cell Biol. 25, 637-651.
96. Zhou, P., Derkatch, I. L., Uptain, S. M., Patino, M. M., Lindquist, S., and Liebman, S. W. (1999). The yeast non-Mendelian factor [ETA + ] is a variant of [PSI + ], a prion-like form of release factor eRF3. EMBO J. 18, 1182-1191.
97. Zhouravleva, G., Frolova, L., Le Goff, X., Le Guellec, R., Inge-Vechtomov, S., Kisselev, L., and Philippe, M. (1995). Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065-4072.
98. Zhu, B., Mandal, S. S., Pham, A. D., Zheng, Y., Erdjument-Bromage, H., Batra, S. K., Tempst, P., and Reinberg, D. (2005). The human PAF complex coordinates transcription with events downstream of RNA synthesis. Genes Dev. 19, 1668-1673.