Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)- binding protein, regulates polyadenylation

Molecular and Cellular Biology

Volumn 18, Issue 12, 1998, Pages 7383-7396

  Mangus, David A ^a   Amrani, Nadia ^a   Jacobson, Allan ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMITROLE; BINDING PROTEIN; INITIATION FACTOR; MESSENGER RNA; SUCROSE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL NUCLEUS; CELL VIABILITY; CONCENTRATION RESPONSE; CONTROLLED STUDY; GENE EXPRESSION REGULATION; GENE REPRESSION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYADENYLATION; POLYSOME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REPORTER GENE; RNA CLEAVAGE; RNA DEGRADATION; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE; SUPPRESSOR GENE; TRANSLATION INITIATION; TRANSLATION REGULATION;

SACCHAROMYCES CEREVISIAE;

EID: 0031724595     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.12.7383     Document Type: Article

References (81)

1. Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
2. Altschul, S. F., T. L. Madden, A. A. Schäffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
3. Amrani, N., M. E. Dufour, N. Bonneaud, and F. Lacroute. 1996. Mutations in STS1 suppress the defect in 3′ mRNA processing caused by the ma15-2 mutation in Saccharomyces cerevisiae. Mol. Gen. Genet. 252:552-562.
4. Amrani, N., M. Minet, M. Le Gouar, F. Lacroute, and F. Wyers. 1997. Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) length in vitro. Mol. Cell. Biol. 17:3694-3701.
5. Antonsson, B., S. Montessuit, L. Friedli, M. A. Payton, and G. Paravicini. 1994. Protein kinase C in yeast. J. Biol. Chem. 269:16281-16288.
6. Baer, B. W., and R. D. Kornberg. 1980. Repeating structure of cytoplasmic poly(A)-ribonucleoprotein. Proc. Natl. Acad. Sci. USA 77:1890-1892.
7. Baer, B. W., and R. D. Kornberg. 1983. The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein. J. Cell Biol. 96:717-721.
8. Baim, S. B., D. F. Pietras, D. C. Eustice, and F. Sherman. 1985. A mutation allowing an mRNA secondary structure diminishes translation of Sacchammyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol. 5:1839-1846.
9. Bartel, P. L., and S. Fields (ed.). 1997. The yeast two-hybrid system. Oxford University Press, New York, N.Y.
10. Bartel, P. L., C. Chien, R. Sternglanz, and S. Fields. 1993. Using the two-hybrid system to detect protein-protein interactions, p. 153-179. In D. A. Hartley '(ed.), Cellular interactions in development: a practical approach. IRL Press, Oxford, England.
11. Baudin, A., K. O. Ozier, A. Denouel, F. Lacroute, and C. Cullin. 1993. A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res. 21:3329-3330.
12. Beelman, C. A., A. Stevens, G. Caponigro, T. E. LaGrandeur, L. Hatfield, and R. Parker. 1996. An essential component of the decapping enzyme required for normal rates of mRNA turnover. Nature 382:642-646.
13. Boeck, R., S. Tarun, M. Rieger, J. A. Deardorff, S. Müller-Auer, and A. B. Sachs. 1996. The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. J. Biol. Chem. 271:432-438.
14. Breeden, L., and K. Nasmyth. 1985. Regulation of the yeast HO gene. Cold Spring Harbor Symp. Quant. Biol. 50:643-650.
15. Brown, C. E., S. Z. Tarun, R. Boeck, and A. B. Sachs. 1996. PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:5744-5753.
16. Caponigro, G., and R. Parker. 1995. Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev. 9:2421-2432.
17. Caponigro, G., and R. Parker. 1996. Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae. Microbiol. Rev. 60:233-249.
18. Chen, J., and C. Moore. 1992. Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA. Mol. Cell. Biol. 12:3470-3481.
19. Craig, A. W. B., A. Haghighat, A. T. K. Yu, and N. Sonenberg. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392:520-523.
20. Dominski, Z., J. Sumerel, R. J. Hanson, and W. F. Marzluff. 1995. The polyribosomal protein bound to the 3′ end of histone mRNA can function in histone pre-mRNA processing. RNA 1:915-923.
21. Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
22. Gallie, D. R., N. J. Lewis, and W. F. Marzluff. 1996. The histone 3′-terminal stem-loop is necessary for translation in Chinese hamster ovary cells. Nucleic Acids Res. 24:1954-1962.
23. Garrels, J. I. 1995. YPD - a database for the proteins of Saccharomyces cerevisiae. Nucleic Acids Res. 24:46-49.
24. Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-360.
25. Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
26. Guthrie, C., and G. R. Fink (ed.). 1991. Methods in enzymology: molecular biology of Saccharomyces cerevisiae. Academic Press, Inc., New York, N.Y.
27. Hanson, R. J., J.-H. Sun, D. G. Willis, and W. F. Marzluff. 1996. Efficient extraction and partial purification of the polyribosomal-associated stem-loop binding protein bound to the 3′ end of histone mRNA. Biochemistry 35: 2146-2156.
28. Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
29. Hatfield, L., C. A. Beelman, A. Stevens, and R. Parker. 1996. Mutations in trans-acting factors affecting mRNA decay in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:5830-5838.
30. Herrick, D., R. Parker, and A. Jacobson. 1990. Identification and comparison of stable and unstable mRNAs in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 10:2269-2284.
31. Hollenberg, S. M., R. Sternglanz, P. F. Cheng, and H. Weintraub. 1995. Identification of a new family of tissue-specific base helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15:3813-3822.
32. Holm, C., D. W. Meeks-Wagner, W. L. Fangman, and D. Botstein. 1986. A rapid, efficient method for isolating DNA from yeast. Gene 42:169-173.
33. + RNA. Methods Enzymol. 152:254-261.
34. Jacobson, A. 1996. Poly(A) metabolism and translation: the closed loop model, p. 451-480. In J. Hershey, M. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
35. James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425-1436.
36. Jones, J. S., and L. Prakash. 1990. Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast 6:363-366.
37. Kessler, M. M., M. F. Henry, E. Shen, J. Zhao, S. Gross, P. A. Silver, and C. L. Moore. 1997. Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′-end formation in yeast. Genes Dev. 11:2545-2556.
38. Kessler, S. H., and A. B. Sachs. 1998. RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 18:51-57.
39. Kneller, D. G., F. E. Cohen, and R. Langridge. 1990. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 214:171-182.
40. Koch, C. A., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. 1991. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252:668-674.
41. Kuhn, U., and T. Pieler. 1996. Xenopus poly(A)-binding protein: functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256: 20-30.
42. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
43. Levin, D. E., F. O. Fields, R. Kunisawa, J. M. Bishop, and J. Thorner. 1990. A candidate protein kinase C gene. PKC1, is required for the S. cerevisiae cell cycle. Cell 62:213-224.
44. Lin, R. J., A. J. Newman, S. C. Cheng, and J. Abelson. 1985. Yeast mRNA splicing in vitro. J. Biol. Chem. 260:14780-14792.
45. Lowell, J. E., D. Z. Rudner, and A. B. Sachs. 1992. 3′-UTR-dependent deadenylation by the yeast poly(A) nuclease. Genes Dev. 6:2088-2099.
46. Mangus, D. A., and A. Jacobson. Unpublished observations.
47. Manrow, R. E., and A. Jacobson. 1986. Identification and characterization of developmentally regulated mRNP proteins of Dictyostelium discoideum. Dev. Biol. 116:213-227.
48. Marzluff, W. F. 1992. Histone 3′ ends: essential and regulatory functions. Gene Expression 2:93-97.
49. Metzler, W. J., A. J. Bell, E. Ernst, T. B. Lavoie, and L. Mueller. 1994. Identification of the poly-L-proline binding site on human profilin. J. Biol. Chem. 269:4620-4625.
50. Minvielle-Sebastia, L., P. J. Preker, T. Wiederkehr, Y. Strahm, and W. Keller. 1997. The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3′-end formation. Proc. Natl. Acad. Sci. USA 94:7897-7902.
51. Muhlrad, D., R. Hunter, and R. Parker. 1992. A rapid method for the localized mutagenesis of yeast genes. Yeast 8:79-82.
52. Pain, V. M. 1996. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236:747-771.
53. Pandey, N. B., J.-H. Sun, and W. F. Marzluff. 1991. Different complexes are formed on the 3′ end of histone mRNA in nuclear and polysomal extracts. Nucleic Acids Res. 19:5653-5659.
54. Peltz, S. W., J. L. Donahue, and A. Jacobson. 1992. A mutation in tRNA nucleotidyltransferase stabilizes mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 12:5778-5784.
55. Proweller, A., and J. S. Butler. 1996. Ribosomal association of poly(A)-binding protein in poly(A)-deficient Saccharomyces cerevisiae. J. Biol. Chem. 271:10859-10865.
56. Pulst, S. M., A. Nechiporuk, T. Nechiporuk, S. Gispert, X. N. Chen, I. LopesCendes, S. Pearlman, S. Starkman, G. Orozco-Diaz, A. Lunkes, P. Dejong, G. A. Rouleau, G. Auburger, J. R. Korenberg, C. Figueroa, and S. Sahba. 1996. Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2. Nat. Genet. 14:269-276.
57. Roemer, T., S. Delaney, and H. Bussey. 1993. SKN1 and KRE6 define a pair of functional homologs encoding putative membrane proteins involved in β-glucan synthesis. Mol. Cell. Biol. 13:4039-4048.
58. Roemer, T., G. Paravicini, M. A. Payton, and H. Bussey. 1994. Characterization of the yeast (1→6)-β-glucan biosynthetic components, Kre6p and Skn1p, and genetic interactions between the PKC1 pathway and extracellular matrix assembly. J. Cell Biol. 127:567-579.
59. Rose, M. D., F. Winston, and P. Heiter. 1990. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
60. Ross-Macdonald, P., D. Simoniatis, and M. Snyder. Personal communication.
61. Sachs, A. 1990. The role of poly(A) in the translation and stability of mRNA. Curr. Opin. Cell Biol. 2:1092-1098.
62. Sachs, A. Personal communication.
63. Sachs, A. B., M. W. Bond, and R. D. Kornberg. 1986. A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell 45:827-835.
64. Sachs, A. B., and R. W. Davis. 1989. The poly(A)-binding protein is required for poly(A) shortening and 60S ribosomal subunit dependent translation initiation. Cell 58:857-867.
65. Sachs, A. B., and R. W. Davis. 1990. Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science 247:1077-1079.
66. Sachs, A. B., R. W. Davis, and R. D. Kornberg. 1987. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol. Cell. Biol. 7:3268-3276.
67. Sachs, A. B., and J. A. Deardorff. 1992. Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast. Cell 70:961-973.
68. Sachs, A. B., P. Sarnow, and M. W. Hentze. 1997. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89:831-838.
69. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
70. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
71. Schlüter, C., M. Duchrow, C. Wohlenberg, M. H. G. Becker, G. Key, H.-D. Flad, and J. Gerdes. 1993. The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins. J. Cell Biol. 123:513-522.
72. Soni, R., J. P. Carmichael, and J. A. H. Murray. 1993. Parameters affecting lithium acetate-mediated transformation of Saccharomyces cerevisiae and development of a rapid and simple procedure. Curr. Genet. 24: 455-459.
73. Steel, L. F., and A. Jacobson. 1987. Translational control of ribosomal protein synthesis during early Dictyostelium discoideum development. Mol. Cell. Biol. 7:965-972.
74. Tarun, S. Z., and A. B. Sachs. 1995. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9:2997-3007.
75. Tarun, S. Z., and A. B. Sachs. 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15:7168-7177.
76. Tarun, S. Z., S. E. Wells, J. A. Deardorff, and A. B. Sachs. 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94:9046-9051.
77. Vogel, H. J., and D. M. Bonner. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
78. Wang, Z.-F., M. L. Whitfield, T. C. Ingledue III, Z. Dominski, and W. F. Marzluff. 1996. The protein that binds the 3′ end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing. Genes Dev. 10:3028-3040.
79. Watanabe, M., C.-Y. Chen, and D. Levin. 1994. Saccharomyces cerevisiae PKC1 encodes a protein kinase C (PKC) homolog with a substrate specificity similar to that of mammalian PKC. J. Biol. Chem. 269:16829-16836.
80. White, T. J., N. Arnheim, and H. A. Erlich. 1989. The polymerase chain reaction. Trends Genet. 5:185-189.
81. Wickens, M., J. Kimble, and S. Strickland. 1996. Translational control of developmental decisions, p. 411-450. In J. Hershey, M. Mathews, and N. Sonenherg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.