Structure and function of poly(A) binding proteins

Biochimica et Biophysica Acta - Gene Structure and Expression

Volumn 1678, Issue 2-3, 2004, Pages 67-84

  Kühn, Uwe ^a   Wahle, Elmar ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

3 end processing; mRNA turnover; Poly(A) binding protein

Indexed keywords

MESSENGER RNA; POLYADENYLIC ACID BINDING PROTEIN;

CYTOPLASM; EUKARYOTE; GENE CONTROL; NONHUMAN; NUCLEOTIDE SEQUENCE; OCULOPHARYNGEAL MUSCULAR DYSTROPHY; POLYADENYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; TRANSLATION INITIATION;

ANIMALS; CELL NUCLEUS; CYTOPLASM; FUNGAL PROTEINS; HUMANS; MODELS, BIOLOGICAL; POLY(A)-BINDING PROTEIN I; POLY(A)-BINDING PROTEIN II; POLY(A)-BINDING PROTEINS; PROTEIN BINDING; RNA, MESSENGER; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EUKARYOTA;

EID: 2442482777     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2004.03.008     Document Type: Review

References (202)

1. Blobel G. A protein of molecular weight 78, 000 bound to the polyadenylate region of eukaryotic messenger RNAs. Proc. Natl. Acad. Sci. U. S. A. 70:1973;924-928
2. Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., Dreyfuss G. mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol. Cell. Biol. 6:1986;2932-2943
3. Sachs A.B., Bond M.W., Kornberg R.D. A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell. 45:1986;827-835
4. Nemeth A., Krause S., Blank D., Jenny A., Jenö P., Lustig A., Wahle E. Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II. Nucleic Acids Res. 23:1995;4034-4041
5. Wahle E. A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell. 66:1991;759-768
6. Winstall E., Sadowski M., Kühn U., Wahle E., Sachs A.B. The Saccharomyces cerevisiae RNA-binding protein Rbp29 functions in cytoplasmic mRNA metabolism. J. Biol. Chem. 275:2000;21817-21826
7. Görlach M., Burd C.G., Dreyfuss G. The mRNA poly(A)-binding protein: localization, abundance and RNA-binding specificity. Exp. Cell Res. 211:1994;400-407
8. Krause S., Fakan S., Weis K., Wahle E. Immunodetection of poly(A) binding protein II in the cell nucleus. Exp. Cell Res. 214:1994;75-82
9. Voeltz G.K., Ongkasuwan J., Standart N., Steitz J.A. A novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts. Genes Dev. 15:2001;774-788
10. Mangus D.A., Evans M.C., Jacobson A. Poly(A) binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4:2003;223-236
11. Grange T., Martins de Sa C., Oddos J., Pictet R. Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif. Nucleic Acids Res. 15:1987;4771-4787
12. Kühn U., Pieler T. Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256:1996;20-30
13. Nietfeld W., Mentzel H., Pieler T. Teh Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains. EMBO J. 9:1990;3699-3705
14. Lee J., Bedford M.T. PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays. EMBO Rep. 3:2002;268-273
15. Burd C.G., Matunis E.L., Dreyfuss G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11:1991;3419-3424
16. Sachs A.B., Davis R.W., Kornberg R.D. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol. Cell. Biol. 7:1987;3268-3276
17. Baer B.W., Kornberg R.D. The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein. J. Cell Biol. 96:1983;717-721
18. Deardorff J.A., Sachs A.B. Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A) binding protein. J. Mol. Biol. 269:1997;67-81
19. Swanson M.S., Dreyfuss G. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 8:1988;2237-2241
20. Melo E.O., Dhalia R., Martins de Sa C., Standart N., de Melo Neto O.P. Identification of a C-terminal PABP-PABP interaction domain: role in cooperative binding to poly(A) and efficient cap distal translational repression. J. Biol. Chem. 278:2003;46357-46368
21. Le H., Browning K.S., Gallie D.R. The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B. J. Biol. Chem. 275:2000;17452-17462
22. Dreyfuss G., Swanson M.S., Pinol-Roma S. Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation. Trends Biochem. Sci. 13:1988;86-91
23. Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K. Recognition of polyadenylate RNA by the poly(A) binding protein. Cell. 98:1999;835-845
24. Saenger W. Principles of Nucleic Acid Structure. 1983;Springer, New York
25. Sladic R.T., Lagnado C.A., Bagley C.J., Goodall G.J. Human PABP binds AU-rich RNA via RNA-binding domains 3 and 4. Eur. J. Biochem. 271:2004;450-457
26. Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I., Sprules T., Gehring K. Solution structure of the orphan PABPC domain from Saccharomyces cerevisiae poly(A)-binding protein. J. Biol. Chem. 277:2002;22822-22828
27. Kozlov G., Trempe J.-F., Khaleghpour K., Kahvedjian A., Ekiel I., Gehring K. Structure and function of the C-terminal PABC domain of human poly(A)-binding protein. Proc. Natl. Acad. Sci. U. S. A. 98:2001;4409-4413
28. Siddiqui N., Kozlov G., D'Orso I., Trempe J.-F., Gehring K. Solution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: a vegetal PABPC domain. Protein Sci. 12:2003;1925-1933
29. Deo R.C., Sonenberg N., Burley S.K. X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein. Proc. Natl. Acad. Sci. U. S. A. 98:2001;4414-4419
30. Kozlov G., De Crescenzo G., Lim N.S., Siddiqui N., Fantus D., Kahvejian A., Trempe J.-F., Elias D., Ekiel I., Sonenberg N., O'Connor-McCourt M., Gehring K. Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase. EMBO J. 23:2004;272-281
31. Munroe D., Jacobson A. Tales of poly(A): a review. Gene. 91:1990;151-158
32. Proweller A., Butler S. Efficient translation of poly(A)-deficient mRNAs in Saccharomyces cerevisiae. Genes Dev. 8:1994;2629-2640
33. Searfoss A., Wickner R. 3′ Poly(A) is dispensable for translation. Proc. Natl. Acad. Sci. U. S. A. 97:2000;9133-9137
34. Preiss T., Hentze M.W. Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature. 392:1998;516-520
35. - mRNA during translation initiation in Saccharomyces cerevisiae. J. Biol. Chem. 272:1997;6004-6010
36. Sachs A.B., Davis R.W. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell. 58:1989;857-867
37. Sachs A.B., Davis R.W. Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science. 247:1990;1077-1079
38. Kahvejian A., Roy G., Sonenberg N. The mRNA closed-loop model: the function of PABP and PABP-interacting proteins in mRNA translation. Cold Spring Harbor Symp. Quant. Biol. 66:2001;293-300
39. Gallie D.R. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5:1991;2108-2116
40. Iizuka N., Najita L., Franzusoff A., Sarnow P. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell. Biol. 14:1994;7320-7322
41. Tarun S.Z., Sachs A.B. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9:1995;2997-3007
42. Gebauer F., Corona D.F.V., Preiss T., Becker P.B., Hentze M.W. Translational control of dosage compensation in Drosophila by sex-lethal: cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail. EMBO J. 18:1999;6146-6154
43. Bergamini G., Preiss T., Hentze M.W. Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system. RNA. 6:2000;1781-1790
44. Borman A.M., Michel Y.M., Kean K.M. Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′ end. Nucleic Acids Res. 28:2000;4068-4075
45. Michel Y.M., Poncet D., Piron M., Kean K.M., Borman A.M. Cap-poly(A) synergy in mammalian cell-free extracts. J. Biol. Chem. 275:2000;32268-32276
46. Hershey J.W.B., Merrick W.C. Pathway and mechanism of initiation of protein synthesis. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;33-88 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
47. Gingras A.-C., Raught B., Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:1999;913-963
48. Sachs A.B., Sarnow P., Hentze M.W. Starting at the beginning, middle and end: translation initiation in eukaryotes. Cell. 89:1997;831-838
49. Sachs A.B., Varani G. Eukaryotic translation initiation: there are (at least) two sides to every story. Nat. Struct. Biol. 7:2000;356-361
50. Sachs A.B. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;447-465 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
51. Tarun S.Z., Sachs A.B. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15:1996;7168-7177
52. Tarun S.Z., Wells S.E., Deardorff J.A., Sachs A.B. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. U. S. A. 84:1997;9046-9051
53. Le H., Tanguay R.L., Balasta M.L., Wei C.-C., Browning K.S., Metz A.M., Goss D.J., Gallie D.R. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J. Biol. Chem. 272:1997;16247-16255
54. Imataka H., Gradi A., Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17:1998;7480-7489
55. Piron M., Vende P., Cohen J., Poncet D. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4. EMBO J. 17:1998;5811-5821
56. Cao Q., Richter J.D. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21:2002;3852-3862
57. Fraser C.S., Pain V.M., Morley S.J. The association of initiation factor 4F with poly(A)-binding protein is enhanced in serum-stimulated Xenopus kidney cells. J. Biol. Chem. 274:1999;196-204
58. Wakiyama H., Imataka H., Sonenberg N. Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation. Curr. Biol. 10:2000;1147-1150
59. Kessler S.H., Sachs A.B. RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 18:1998;51-57
60. Otero L.J., Ashe M.P., Sachs A.B. The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBO J. 18:1999;3153-3163
61. Gray N.K., Coller J.M., Dickson K.S., Wickens M.P. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19:2000;4723-4733
62. Luo Y., Goss D.J. Homeostasis in mRNA initiation. J. Biol. Chem. 276:2001;43083-43086
63. Wei C.-C., Balasta M.L., Ren J., Goss D.J. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues. Biochemist. 37:1998;1910-1916
64. Mazumder B., Seshadri V., Imataka H., Sonenberg N., Fox P.L. Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 21:2001;6440-6449
65. Herschlag D., Johnson F.B. Synergism in transcriptional activation: a kinetic view. Genes Dev. 7:1993;173-179
66. Wells S.E., Hillner P.E., Vale R.D., Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell. 2:1998;135-140
67. Galili G., Kawata E.E., Smith L.D., Larkin B.A. Role of the 3′-poly(A) sequence in translational regulation of mRNAs in Xenopus laevis oocytes. J. Biol. Chem. 263:1988;5764-5770
68. Cosson B., Berkova N., Couturier A., Chabelskaya S., Philippe M., Zhouravleva G. Poly(A)-binding protein and eRF3 are associated in vivo in human and Xenopus cells. Biol. Cell. 94:2002;205-216
69. Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S., Philippe M., Zhouravleva G. Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence PSI+ propagation. Mol. Cell. Biol. 22:2002;3301-3315
70. Hoshino S., Imai M., Kobayashi T., Uchida N., Katada T. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA. J. Biol. Chem. 274:1999;16677-16680
71. Uchida N., Hoshino S., Imataka H., Sonenberg N., Katada T. A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation. J. Biol. Chem. 277:2002;50286-50292
72. Vende P., Piron M., Castagné N., Poncet D. Efficient translation of rotavirus mRNA requires simultaneous interaction of NSP3 with the eukaryotic translation initiation factor eIF4G and the mRNA 3′ end. Mol. Cell. Biol. 74:2000;7064-7071
73. Groft C.M., Burley S.K. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Mol. Cell. 9:2002;1273-1283
74. Ling J., Morley S.J., Pain V.M., Marzluff W.F., Gallie D.R. The histone 3′-terminal stem-loop binding protein enhances translation through a functional and physical interaction with eukaryotic initiation factor 4G (eIF4G) and eIF3. Mol. Cell. Biol. 22:2002;7853-7867
75. Sanchez R., Marzluff W.F. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol. Cell. Biol. 22:2002;7093-7104
76. Herold J., Andino R. Poliovirus RNA replication requires genome circularization through a protein-protein bridge. Mol. Cell. 7:2001;581-591
77. Guo L., Allen E.M., Miller W.A. Base-pairing between untranslated regions facilitates translation of uncapped, nonpolyadenylated viral RNA. Mol. Cell. 7:2001;1103-1109
78. Jackson R.J. A comparative view of initiation site selection mechanisms. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;127-183 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
79. Michel Y.M., Borman A.M., Paulous S., Kean K.M. Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation. Mol. Cell. Biol. 21:2001;4097-4109
80. Svitkin Y.V., Imataka H., Khaleghpour K., Kahvejian A., Liebig H.-D., Sonenberg N. Poly(A)-binding protein interaction with eIF4G stimulates picornavirus IRES-dependent translation. RNA. 7:2001;1743-1752
81. Searfoss A., Dever T.E., Wickner R. Linking the 3′ poly(A) tail to the subunit joining step of translation initiation: relations of Pab1p, eukaryotic translation initiation factor 5B (Fun12p), and Ski2p-Slh1p. Mol. Cell. Biol. 21:2001;4900-4908
82. Munroe D., Jacobson A. mRNA poly(A) tail, a 3′ enhancer of translational initiation. Mol. Cell. Biol. 10:1990;3441-3455
83. Proweller A., Butler J.S. Ribosomal association of poly(A) binding protein in poly(A)-deficient Saccharomyces cerevisiae. J. Biol. Chem. 271:1996;10859-10865
84. Hensold J.O., Barth-Baus D., Stratton C.A. Inducers of erythroleukemic differentiation cause messenger RNAs that lack poly(A)-binding protein to accumulate in translationally inactive, salt-labile 80S ribosomal complexes. J. Biol. Chem. 271:1996;23246-23254
85. Bushell M., Wood W., Carpenter G., Pain V.M., Morley S.J., Clemens M.J. Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages. J. Biol. Chem. 276:2001;23922-23928
86. Bi X., Goss D.J. Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F. J. Biol. Chem. 275:2000;17740-17746
87. Benard L., Carroll K., Valle R.C.P., Wickner R. Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis. Mol. Cell. Biol. 18:1998;2688-2696
88. - mRNA surveillance by a yeast antiviral system. Mol. Cell. Biol. 15:1995;2763-2771
89. Brown J.T., Johnson A.W. A cis-acting element known to block 3′ mRNA degradation enhances expression of poly(A)-minus mRNA in wild-type yeast cells and phenocopies a ski mutant. RNA. 7:2001;1566-1577
90. Joachims M., Van Breughel P.C., Lloyd R.E. Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J. Virol. 73:1999;718-727
91. Kerekatte V., Keiper B.D., Badorff C., Cai A., Knowlton K.U., Rhoads R.E. Cleavage of poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff? J. Virol. 73:1999;709-717
92. Kuyumcu-Martinez N.M., Joachims M., Lloyd R.E. Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J. Virol. 76:2002;2062-2074
93. Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N. Paip1 interacts with poly(A) binding protein through two independent binding motifs. Mol. Cell. Biol. 22:2002;3769-3782
94. Craig A.W.B., Haghigat A., Yu A.T.K., Sonenberg N. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature. 392:1998;520-523
95. Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N. Translational repression by a novel partner of human poly(A) binding protein, Paip2. Mol. Cell. 7:2001;205-216
96. Roy G., Miron M., Khaleghpour K., Lasko P., Sonenberg N. The Drosophila poly(A) binding protine-interacting protein, Paip2, is a novel effector of cell growth. Mol. Cell. Biol. 24:2004;1143-1154
97. Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N. Dual interactions of the translational repressor Paip2 with poly(A) binding protein. Mol. Cell. Biol. 21:2001;5200-5213
98. Richter J.D. Influence of polyadenylation-induced translation on metzoan development and neuronal synaptic function. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;785-807 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
99. Preiss T., Muckenthaler M., Hentze M.W. Poly(A)-tail-promoted translation in yeast: implications for translational control. RNA. 4:1998;1321-1331
100. Caponigro G., Parker R. Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae. Microbiol. Rev. 60:1996;233-249
101. Parker R., Song H. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 11:2004;121-127
102. Tucker M., Parker R. Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae. Annu. Rev. Biochem. 69:2000;571-595
103. Caponigro G., Parker R. Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev. 9:1995;2421-2432
104. Lowell J.E., Rudner D.Z., Sachs A.B. 3′-UTR-dependent deadenylation by the yeast poly(A) nuclease. Genes Dev. 6:1992;2088-2099
105. Boeck R., Tarun S., Rieger M., Deardorff J.A., Müller-Auer S., Sachs A.B. The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. J. Biol. Chem. 271:1996;432-438
106. Brown C.E., Tarun S.Z., Boeck R., Sachs A.B. PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:1996;5744-5753
107. Uchida N., Hoshino S., Katada T. Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein. J. Biol. Chem. 279:2003;1383-1391
108. Mangus D.A., Amrani N., Jacobson A. Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mol. Cell. Biol. 18:1998;7383-7396
109. Tucker M., Valencia-Sanchez M.A., Staples R.R., Chen J., Denis C.L., Parker R. The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell. 104:2001;377-386
110. Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R. Ccr4p is the catalytic subunit of a Ccr4p/Pop2/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. EMBO J. 21:2002;1427-1436
111. Wormington M., Searfoss A.M., Hurney C.A. Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes. EMBO J. 15:1996;900-909
112. Körner C.G., Wormington M., Muckenthaler M., Schneider S., Dehlin E., Wahle E. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 17:1998;5427-5437
113. Körner C., Wahle E. Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease. J. Biol. Chem. 272:1997;10448-10456
114. Bernstein P., Peltz S.W., Ross J. The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol. Cell. Biol. 9:1989;659-670
115. Gao M., Fritz D.T., Ford L.P., Wilusz J. Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro. Mol. Cell. 5:2000;479-488
116. Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B. A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell. 103:2000;29-40
117. Coller J.M., Gray N.K., Wickens M.P. mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation. Genes Dev. 12:1998;3226-3235
118. van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Séraphin B. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21:2002;6915-6924
119. Wang Z., Jiao X., Carr-Schmid A., Kiledjian M. The hDcp2 protein is a mammalian mRNA decapping enzyme. Proc. Natl. Acad. Sci. U. S. A. 99:2002;12663-12668
120. Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA. 7:2001;1717-1727
121. Dunckley T., Tucker M., Parker R. Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics. 157:2001;27-37
122. Kshirsagar M., Parker R. Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae. Genetics. 166:2004;729-739
123. Schwartz D.C., Parker R. Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:1999;5247-5256
124. Schwartz D.C., Parker R. mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 20:2000;7033-7942
125. Wilusz C.J., Gao M., Jones C.L., Wilusz J., Peltz S.W. Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts. RNA. 7:2001;1416-1424
126. Tharun S., Parker R. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell. 8:2001;1075-1083
127. He W., Parker R. Functions of Lsm proteins in mRNA degradation and splicing. Curr. Opin. Cell Biol. 12:2000;346-350
128. He W., Parker R. The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3′ termini from partial degradation. Genetics. 158:2001;1445-1455
129. Wang Z., Kiledjian M. The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity. Mol. Cell. Biol. 20:2000;6334-6341
130. Brown J.T., Yang X., Johnson A.W. Inhibition of mRNA turnover in yeast by an xrn1 mutation enhances the requirement for eIF4E binding to eIF4G and for proper capping of transcripts by Ceg1p. Genetics. 155:2000;31-42
131. Morrissey J.P., Deardorff J.A., Hebron C., Sachs A.B. Decapping of stabilized, polyadenylated mRNA in yeast pab1 mutants. Yeast. 15:1999;687-702
132. Boeck R., Lapeyre B., Brown C.E., Sachs A.B. Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant. Mol. Cell. Biol. 18:1998;5062-5072
133. Bonnerot C., Boeck R., Lapeyre B. The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20:2000;5939-5946
134. Hatfield L., Beelman C.A., Stevens A., Parker R. Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:1996;5830-5838
135. Wyers F., Minet M., Dufour M.E., Vo L.T.A., Lacroute F. Deletion of the PAT1 gne affects translation initiation and suppresses a PAB1 gene deletion in yeast. Mol. Cell. Biol. 20:2000;3538-3549
136. Chekanova J.A., Shaw R.J., Belostotsky D.A. Analysis of an essential requirement for the poly(A) binding protein function using cross-species complementation. Curr. Biol. 11:2001;1207-1214
137. Chekanova J.A., Belostotsky D.A. Evidence that poly(A) binding protein has an evolutionarily conserved function in facilitating mRNA biogenesis and export. RNA. 9:2003;1476-1490
138. Belostotsky D.A. Unexpected complexity of poly(A)-binding protein gene families in flowering plants: three conserved lineages that are at least 200 million years old and possible auto- and cross-regulation. Genetics. 163:2003;311-319
139. de Melo Neto O.P., Standart N., Martins de Sa C. Autoregulation of poly(A)-binding protein synthesis in vitro. Nucleic Acids Res. 23:1995;2198-2205
140. Wu J., Bag J. Negative control of the poly(A)-binding protein mRNA translation is mediated by the adenine-rich region of its 5′-untranslated region. J. Biol. Chem. 273:1998;34535-34542
141. Bag J. Feedback inhibition of poly(A)-binding protein mRNA translation. J. Biol. Chem. 276:2001;47352-47360
142. Melo E.O., de Melo Neto O.P., Martins de Sa C. Adenosine-rich elements present in the 5′-untranslated region of PABP mRNA can selectively reduce the abundance and translation of CAT mRNAs in vivo. FEBS Lett. 546:2003;329-334
143. Meyuhas O., Hornstein E. Translational control of TOP mRNAs. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;671-693 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
144. Hornstein E., Git A., Braunstein I., Avni D., Meyuhas O. The expression of poly(A)-binding protein gene is translationally regulated in a growth-dependent fashion through a 5′-terminal oligopyrimidine tract motif. J. Biol. Chem. 274:1999;1708-1714
145. Féral C., Guellaen G., Pawlak A. Human testis expresses a specific poly(A)-binding protein. Nucleic Acids Res. 29:2001;1872-1883
146. Yang H., Duckett C.S., Lindsten T. iPABP, an inducible poly(A)-binding protein detected in activated human T cells. Mol. Cell. Biol. 15:1995;6770-6776
147. Blanco P., Sargent C.A., Boucher C.A., Howell G., Ross M., Affara N.A. A novel poly(A) binding protein gene (PABPC5) maps to an X-specific subinterval in the Xq21.3/Yp11.2 homology block of the human sex chromosomes. Genomics. 74:2001;1-11
148. Cosson B., Couturier A., Le Guellec R., Moreau J., Chabelskaya S., Zhouravleva G., Philippe M. Characterization of the poly(A) binding proteins expressed during oogenesis and early development of Xenopus laevis. Biol. Cell. 94:2002;217-231
149. Brais B., Bouchard J.P., Xie Y.G., Rochefort D.L., Chrétien N., Tomé F.M.S., Lafrenière R.G., Rommens J.M., Uyama E., Nohira O., Blumen S., Korcyn A.D., Heutink P., Mathieu J., Duranceau A., Codère F., Fardeau M., Rouleau G.A. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat. Genet. 18:1998;164-167
150. Kerwitz Y., Kühn U., Lilie H., Knoth A., Scheuermann T., Friedrich H., Schwarz E., Wahle E. Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA. EMBO J. 22:2003;3705-3714
151. Smith J.J., Rücknagel K.P., Schierhorn A., Tang J., Nemeth A., Linder M., Herschman H.R., Wahle E. Unusual sites of arginine methylation in poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J. Biol. Chem. 274:1999;13229-13234
152. Burd C.G., Dreyfuss G. Conserved structure and diversity of functions of RNA-binding proteins. Science. 265:1994;615-621
153. Meyer S., Urbanke C., Wahle E. Equilibrium studies on the association of the nuclear poly(A) binding protein with poly(A) of different lengths. Biochemistry. 41:2002;6082-6089
154. Kühn U., Nemeth A., Meyer S., Wahle E. The RNA binding domains of the nuclear poly(A)-binding protein. J. Biol. Chem. 278:2003;16916-16925
155. Wahle E., Lustig A., Jenö P., Maurer P. Mammalian Poly(A) binding protein II. J. Biol. Chem. 268:1993;2937-2945
156. Keller R.W., Kühn U., Aragon M., Bornikova L., Wahle E., Bear D.G. The Nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail. J. Mol. Biol. 297:2000;569-583
157. Colgan D.F., Manley J.L. Mechanism and regulation of mRNA polyadenylation. Genes Dev. 11:1997;2755-2766
158. Minvielle-Sebastia L., Keller W. mRNA polyadenylation and its coupling to other RNA processing reactions and to transcription. Curr. Opin. Cell Biol. 11:1999;352-357
159. Wahle E., Rueegsegger U. 3′-End processing of pre-mRNA in eukaryotes. FEMS Microbiol. Rev. 23:1999;277-295
160. Zhao J., Hyman L., Moore C. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation and interrelationship with other steps in mRNA synthesis. Microbiol. Mol. Rev. 63:1999;405-445
161. Bienroth S., Keller W., Wahle E. Assembly of a processive messenger RNA polyadenylation complex. EMBO J. 12:1993;585-594
162. Chen Z., Li Y., Krug R.M. Influenza A virus NS1 protein targets the poly(A)-binding protein II of the cellular 3′-end processing machinery. EMBO J. 18:1999;2273-2283
163. Sawicki S.G., Jelinek W., Darnell J.E. 3′-Terminal addition of HeLa cell nuclear and cytoplasmic poly(A). J. Mol. Biol. 113:1977;219-235
164. Wahle E. Poly(A) tail length control is caused by termination of processive synthesis. J. Biol. Chem. 270:1995;2800-2808
165. Calado A., Tomé F.M.S., Brais B., Rouleau G.A., Kühn U., Wahle E., Carmo-Fonseca M. Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum. Mol. Genet. 9:2000;2321-2328
166. Fan X., Dion P., Laganiere J., Brais B., Rouleau G.A. Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death. Hum. Mol. Genet. 10:2001;2341-2351
167. Scheuermann T., Schulz B., Blume A., Wahle E., Rudolph R., Schwarz E. Trinucleotide expansions leading to an extended poly-L-alanine segment in the poly(A) binding protein PABPN1 cause fibril formation. Protein Sci. 12:2003;2685-2692
168. Abu-Baker A., Messaed C., Laganiere J., Gaspar C., Brais B., Rouleau G.A. Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy. Hum. Mol. Genet. 12:2003;2609-2623
169. Bao Y.P., Cook L.J., O'Donovan D., Uyama E., Rubinsztein D.C. Mammalian, yeast, bacterial and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. J. Biol. Chem. 277:2002;12263-12269
170. Hino H., Araki K., Uyama E., Takeya M., Araki M., Yoshinobu K., Miike K., Kawazoe Y., Maeda Y., Uchino M., Yamamura K. Myopathy phenotype in transgenic mice expressing mutated PABPN1 as a model of oculopharyngeal muscular dystrophy. Hum. Mol. Genet. 13:2003;181-190
171. Berciano M.T., Villagra N.T., Ojeda J.L., Navascues J., Gomes A., Lafarga M., Carmo-Fonseca M. Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus. Hum. Mol. Genet. 13:2004;829-838
172. Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K. The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Hum. Mol. Genet. 10:2001;1129-1139
173. Benoit B., Nemeth A., Aulner N., Kühn U., Simonelig M., Wahle E., Bourbon H.-M. The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro. Nucleic Acids Res. 27:1999;3771-3778
174. Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F. Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro. Mol. Cell. Biol. 17:1997;3694-3701
175. Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W. 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. U. S. A. 94:1997;7897-7902
176. Lingner J., Radtke I., Wahle E., Keller W. Purification and characterization of poly(A) polymerase from Saccharomaces cerevisiae. J. Biol. Chem. 266:1991;8741-8746
177. Brown C.E., Sachs A.B. Poly(A) tail length control in Saccharomaces cerevisiae occurs by message-specific deadenylation. Mol. Cell. Biol. 18:1998;6548-6559
178. Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Global analysis of protein localization in budding yeast. Nature. 425:2003;686-691
179. Hector R.E., Nykamp K.R., Dheur S., Anderson J.T., Non P.J., Urbinati C.R., Wilson S.M., Minvielle-Sebastia L., Swanson M.S. Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export. EMBO J. 21:2002;1800-1810
180. Anderson J.T., Wilson S.M., Datar K.V., Swanson M.S. NAB2: a yeast nuclear polyadenylated RNA-Binding protein essential for cell viability. Mol. Cell. Biol. 13:1993;2730-2741
181. Marfatia K.A., Crafton E.B., Green D.M., Corbett A.H. Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear ribonucleoprotein, Nab2p. Dissecting the requirements for Na2p-facilitated poly(A) RNA export. J. Biol. Chem. 278:2003;6731-6740
182. Calado A., Carmo-Fonseca M. Localization of poly(A)-binding protein 2 (PABP2) in nuclear speckles is independent of import into the nucleus and requires binding to poly(A) RNA. J. Cell. Sci. 113:2000;2309-2318
183. Calado A., Kutay U., Kühn U., Wahle E., Carmo-Fonseca M. Deciphering the cellular pathway for transport of poly(A)-binding protein II. RNA. 6:2000;245-256
184. Sachs A.B., Kornberg R.B. Nuclear polyadenylate-binding protein. Mol. Cell. Biol. 5:1985;1993-1996
185. Afonina E., Stauber R., Pavlakis G.N. The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm. J. Biol. Chem. 273:1998;13015-13021
186. Duncan K., Umen J.G., Guthrie C. A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr. Biol. 10:2000;687-696
187. Bear D.G., Fomproix N., Soop T., Björkroth B., Masich S., Daneholt B. Nuclear poly(A)-binding protein PABPN1 is associated with RNA polymerase II during transcription and accompanies the released transcript to the nuclear pore. Exp. Cell Res. 286:2003;332-344
188. Ishigaki Y., Li X., Serin G., Maquat L.E. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell. 106:2001;607-617
189. Calapez A., Pereira H.M., Calado A., Braga J., Rino J., Carvalho C., Tavanez J.P., Wahle E., Rosa A.C., Carmo-Fonseca M. The intranuclear mobility of messenger RNA binding proteins is ATP dependent and temperature sensitive. J. Cell Biol. 159:2002;795-805
190. Düvel K., Valerius O., Mangus D.A., Jacobson A., Braus G.H. Replacement of the yeast TRP4 3′ untranslated region by a hammerhead ribozyme results in a stable and efficiently exported mRNA that lacks a poly(A) tail. RNA. 8:2002;336-344
191. Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C., Cole C.N. Coupling of termination, 3′ processing, and mRNA export. Mol. Cell. Biol. 22:2002;6441-6457
192. Jensen T.H., Dower K., Libri D., Rosbash M. Early formation of mRNA: license for export or quality control? Mol. Cell. 11:2003;1129-1138
193. Gilbert W., Guthrie C. The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA. Mol. Cell. 13:2004;201-212
194. Jarmolowski A., Boelens W.C., Izaurralde E., Mattaj I.W. Nuclear export of different classes of RNA is mediated by specific factors. J. Cell Biol. 124:1994;627-635
195. Ohno M., Segref A., Kuersten S., Mattaj I.W. Identity elements used in export of mRNAs. Mol. Cell. 9:2002;659-671
196. Eckner R., Ellmeier W., Birnstiel M.L. Mature mRNA 3′ end formation stimulates RNA export from the nucleus. EMBO J. 10:1991;3513-3522
197. Huang Y., Carmichael G.G. Role of polyadenylation in nucleocytoplasmic transport of mRNA. Mol. Cell. Biol. 16:1996;1534-1542
198. Poon L.L., Fodor E., Brownlee G.G. Polyuridylated mRNA synthesized by a recombinant influenza virus is defective in nuclear export. J. Virol. 74:2000;418-427
199. Cullen B.R. Nuclear RNA export. J. Cell. Sci. 116:2003;587-597
200. Izaurralde E. Directing mRNA export. Nat. Struct. Biol. Mol. Biol. 11:2004;210-212
201. Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J. Biol. Chem. 277:2002;7752-7760
202. Kenan D.J., Query C.C., Keene J.D. RNA recognition: towards identifying determinants of specificity. Trends Biochem. Sci. 16:1991;214-220