Protein-protein interactions required during translation

Plant Molecular Biology

Volumn 50, Issue 6, 2002, Pages 949-970

  Gallie, Daniel R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Development; Environmental stress; Initiation factors; Phosphorylation; Poly(A) binding protein; Signaling; Translation

Indexed keywords

BIOSYNTHESIS; PROTEINS; RNA;

RIBOSOMES;

PLANTS (BOTANY);

AMINO ACID SEQUENCE; ANIMALS; EUKARYOTIC INITIATION FACTORS; HUMANS; MODELS, BIOLOGICAL; PLANTS; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; RIBOSOMAL PROTEINS; RIBOSOMES; RNA; RNA, MESSENGER; RNA, RIBOSOMAL; RNA, TRANSFER; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0036909438     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021220910664     Document Type: Article

References (151)

1. Abramson, R.D., Browning, K.S., Dever, T.E., Lawson, T.G., Thach, R.E., Ravel, J.M. and Merrick, W.C. 1988. Initiation factors that bind mRNA. A comparison of mammalian factors with wheat germ factors. J. Biol. Chem. 263: 5462-5467.
2. Altmann, M., Muller, P.P., Wittmer, B., Ruchti, F., Lanker, S. and Trachsel, H. 1993. A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity. EMBO J. 12: 3997-4003.
3. Altman, S. and Kirsebom, L. 1999. In: Gesteland, Raymond, F., Cech, Thomas R., Atkins, John F. (eds) Ribonuclease P. The RNA World: The Nature of Modern RNA Suggests a Prebiotic RNA, 2nd Ed. Cold Spring Harbor, N.Y. Cold Spring Harbor Laboratory Press, 1999. Pp. 351-380.
4. Asano, K., Krishnamoorthy, T., Phan, L., Pavitt, G.D. and Hinnebusch, A.G. 1999. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18: 1673-1688.
5. Baer, B.W. and Kornberg, R.D. 1980. Repeating structure of cytoplasmic poly(A)-ribonucleoprotein. Proc. Natl. Acad. Sci. USA 77: 1890-1892.
6. Baker, E.J. 1993. Control of poly(A) length. In: Belasco, J.G. and Brawerman, G. (eds), Control of Messenger RNA Stability. Academic Press, San Diego, CA. Pp. 367-415.
7. Ban, N., Nissen, P., Hansen, J., Moore, P.B. and Steitz, T.A. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Åresolution. Science 289: 905-920.
8. Bandyopadhyay, A. and Maitra, U. 1999. Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): Demonstration that eIF3 interacts with eIF5 in mammalian cells. Nucl. Acids Res. 27: 1331-1337.
9. Barkan, A., Goldschmidt-Clermont, M. 2000. Participation of nuclear genes in chloroplast gene expression. Biochimie 82: 559-572.
10. Beckmann, R.P., Mizzen, L.E. and Welch, W.J. 1990. Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding anal assembly. Science 248: 850-854.
11. Bi, X. and Goss, D.J. 2000. Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4E. J. Biol. Chem. 275: 17740-17746.
12. Bi, X., Ren, J. and Goss, D.J. 2000. Wheat germ translation initiation factor eIF4B affects eIF4A and eIFiso4F helicase activity by increasing the ATP binding affinity of eIF4A. Biochem. 39: 5758-5765.
13. Boorstein, W.R., Ziegelhoffer, T. and Craig, E.A. 1994. Molecular evolution of the HSP70 multigene family. J. Mol. Evol. 38: 1-17.
14. Browning, K.S. 1996. The plant translational apparatus. Plant Mol. Biol. 32: 107-144.
15. Browning, K.S., Lax, S.R. and Ravel, J.M. 1987. Identification of two messenger RNA cap binding proteins in wheat germ. Evidence that the 28-kDa subunit of eIF-4B and the 26-kDa subunit of eIF-4F are antigenically distinct polypeptides. J. Biol. Chem. 262: 11228-11232.
16. Browning, K.S., Fletcher, L., Lax, S.R. and Ravel, J.M. 1989. Evidence that the 59-kDa protein synthesis initiation factor from wheat germ is functionally similar to the 80-kDa initiation factor 4B from mammalian cells. J. Biol. Chem. 264: 8491-8494.
17. Browning, K.S., Webster, C., Roberts, J.K. and Ravel, J.M. 1992. Identification of an isozyme form of protein synthesis initiation factor 4F in plants. J. Biol. Chem. 267: 10096-10100.
18. Browning, K.S., Gallie, D.R., Hershey, J.W., Hinnebusch, A.G., Maitra, U., Merrick, W.C., Norbury, C. 2001. Unified nomenclature for the subunits of eukaryotic initiation factor 3. Trends Biochem. Sci. 26: 284.
19. Bruick, R.K., Mayfield, S.P. 1999. Light-activated translation of chloroplast mRNAs. Trends Plant Sci. 4: 190-195.
20. Burks, E.A., Bezerra, P.P., Le, H., Gallie, D.R. and Browning, K.S. 2001. Plant initiation factor 3 subunit composition resembles mammalian initiation factor 3 and has a novel subunit. J. Biol. Chem. 276: 2122-2131.
21. Bushell, M., Wood, W., Clemens, M.J. and Morley, S.J. 2000. Changes in integrity and association of eukaryotic protein synthesis initiation factors during apoptosis. Eur J. Biochem. 267: 1083-1091.
22. Bushell, M., Wood, W., Carpenter, G., Pain, V.M., Morley, S.J. and Clemens, M.J. 2001. Disruption of the interaction of mammalian protein synthesis initiation factor 4B with the poly(A) binding protein by caspase- and viral protease-mediated cleavages. J. Biol. Chem. 276: 23922-23928.
23. Carberry, S.E. and Goss, D.J. 1991. Wheat germ initiation factors 4F and (iso)4F interact differently with oligoribonucleotide analogues of rabbit α-globin mRNA. Biochem. 30: 4542-4545.
24. Carberry, S.E., Darzynkiewicz, E. and Goss, D.J. 1991. A comparison of the binding of methylated cap analogues to wheat germ protein synthesis initiation factors 4F and (iso)4F. Biochem. 30: 1624-1627.
25. Cech, T.R. and Golden, B.L. 1999. In: Gesteland, Raymond F., Cech. Thomas R., Atkins, John F. (eds), Building a Catalytic Active Site Using Only RNA. The RNA World: The Nature of Modern RNA Suggests a Prebiotic RNA. 2nd Ed. Cold Spring Harbor, N.Y. Cold Spring Harbor Laboratory Press, 1999. Pp. 321-349.
26. Chaudhuri, J., Das, K. and Maitra, U. 1994. Purification and characterization of bacterially expressed mammalian translation initiation factor 5 (eIF-5): Demonstration that eIF-5 forms a specific complex with eIF-2. Biochem. 33: 4794-4799.
27. Chaudhuri, J., Si, K., Maitra, U. 1997. Function of eukaryotic translation initiation factor 1A (eIF1A) (formerly called eIF-4C) in initiation of protein synthesis. J. Biol. Chem. 272: 7883-7891.
28. Chaudhuri, J., Chowdhury, D. and Maitra, U. 1999 Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex. J. Biol. Chem. 274: 17975-17980.
29. Chen, J.-J. 2000. Heme-regulated eIF2α kinase. In: Sonenberg, N., Hershey, J.W.B., Mathews, M.B. (eds), Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp. 529-546.
30. Christensen, A.K., Kahn, L.E. and Bourne, C.M. 1987. Cimular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rate anterior pituitary. Amer. J. Anat. 178: 1-10.
31. Craig, A.W.B., Haghighat, A., Yu, A.T.K. and Sonenberg, N. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392: 520-523.
32. Cuesta, R., Laroia, G. and Schneider, R.J. 2000. Chaperone Hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Devel. 14: 1460-1470.
33. Danon, A. 1997. Translational regulation in the chloroplast. Plant Physiol. 115: 1293-1298.
34. Das, S., Maiti, T., Das, K. and Maitra, U. 1997. Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the β-subunit of eIF2. J. Biol. Chem. 272: 31712-31718.
35. Dorris, D.R., Erickson, F.L. and Hannig E.M. 1995. Mutations in GCD11, the structural gene for eIF-2γ in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis. EMBO J. 14: 2239-2249.
36. Dmwbridge, J., Grainger, J.L. and Winkler, M.W. 1990. Identification and characterization of the poly(A)-binding proteins from the sea urchin: A quantitative analysis. Mol. Cell Biol. 10: 3994-4006
37. Duncan, R. and Hershey, J.W. 1985. Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification. J. Biol. Chem. 260: 5493-5497.
38. Duncan, R.F. and Hershey, J.W. 1989. Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation. J. Cell Biol. 109: 1467-1481.
39. Elliott, R., Pedersen, T.J., Fristensky, B., White, M.J., Dickey, L.F. and Thompson, W.F. 1989. Characterization of a single copy gene encoding ferredoxin I from pea. Plant Cell 1: 681-690.
40. Erickson, F.L. and Hannig, E.M. 1996. Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-subunit. EMBO J. 15: 6311-6320.
41. Flynn, A. and Proud, C.G. 1995. Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells. J. Biol. Chem. 270: 21684-21688.
42. Flynn, A., Oldfield, S. and Proud, C.G. 1993. The role of the β-subunit of initiation factor eIF-2 in initiation complex formation. Biochim. Biophys. Acta 1174: 117-121.
43. Fraser, C.S., Pain, V.W. and Morley, S.J. 1999. The association of initiation factor 4F with poly(A)-binding protein is enhanced in serum-stimulated Xenopus kidney cells. J. Biol. Chem. 274: 196-204.
44. Freire, M.A., Tourneur, C., Granier, F., Camonis, J., El Ammni, A., Browning, K.S., Robaglia, C. 2000. Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein. Plant Mol. Biol. 44: 129-40.
45. Futterer, J. and Hohn, T. 1991. Translation of a polycistronic mRNA in the presence of the cauliflower mosaic virus transactivator protein. EMBO J. 10: 3887-3896.
46. Gallie, D.R. 1991. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Devel. 5: 2108-2116.
47. Gallie, D.R 1996. Translational control of cellular and viral mRNAs. Plant Mol. Biol. 32: 145-158.
48. Gallie, D.R., Browning, K.S. 2001. eIF4G functionally differs from eIFiso4G in promoting internal initiation, cap-independent translation, and translation of structured mRNAs. J. Biol. Chem. 276: 36951-36960.
49. Gallie, D.R. and Tanguay, R. 1994. Poly(A) binds to initiation factors and increases cap-dependent translation in vitro. J. Biol. Chem. 269: 14465-14472.
50. Gallie, D.R., Caldwell, C. and Pitto, L. 1995. Heat shock disrupts cap and poly(A) tail function during translation and increases mRNA stability of introduced reporter mRNA. Plant Physiol. 108: 1703-1713.
51. Gallie, D.R., Le, H., Caldwell, C., Tanguay, R.L., Hoang, N.X. and Browning, K.S. 1997. The phosphorylation state of translation initiation factors is regulated developmentally and following heat shock in wheat. J. Biol. Chem. 272: 1046-1053
52. Gallie, D.R., Ling, J., Niepel, M., Morley, S.J. and Pain, V.M. 2000. The role of 5′-leader length, secondary structure and PABP concentration on cap and poly(A) tail function during translation in Xenopus oocytes. Nucl. Acids Res. 28: 2943-2953.
53. Garcia-Barrio, M.T., Naranda, T., Vazquez de Aldana, C.R., Cuesta, R., Hinnebusch, A.G., Hershey, J.W. and Tamame, M. 1995. GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3. Genes Devel. 9: 1781-1796.
54. Gorlach, M., Burd, C.G. and Dreyfuss, G. 1994. The mRNA poly(A)-binding protein: Localization, abundance, and RNA-binding specificity. Exp. Cell Res. 211: 400-407.
55. Goyer, C., Altmann, M., Lee, H.S., Blanc, A., Deshmukh, M., Woolford, J.L., Trachsel, H. and Sonenberg, N. 1993. TIF4631 and TIF4632 - Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell Biol. 13: 4860-4874.
56. Gradi, A., Imataka, H., Svitkin, Y.V., Rom, E., Raught, B., Morino, S. and Sonenberg, N. 1998. A novel functional human eukaryotic translation initiation factor 4G. Mol. Cell Biol. 18: 334-342.
57. Gray, N.K. and Hentze, M.W. 1994. Iron regulatory protein prevents binding of the 43 S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13(16): 3882-3891.
58. Grifo, J.A., Abramson, R.D., Satler, C.A. and Merrick, W.C. 1984. RNA-stimulated ATPase activity of eukaryotic initiation factors. J. Biol. Chem. 259: 8648-8654.
59. Hershey, J.W.B. and Merrick, W.C. 2000. The pathway and mechanism of initiation of protein synthesis. In: Sonenberg, N., Hershey, J.W.B., Mathews, M.B. (eds.), Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp. 33-88.
60. Hershey, P.E., McWhirter, S.M., Gross, J.D., Wagner, G., Alber, T., Sachs, A.B. 1999. The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. J. Biol. Chem. 274: 21297-21304.
61. Hinnebusch, A.G. 2000. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. In: Sonenberg, N., Hershey, J.W.B., Mathews, M.B. (eds) Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp. 185-243.
62. Horton, L.E., James, P., Craig, E.A. and Hensold, J.O. 2001. The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. J. Biol. Chem. 276: 14426-14433.
63. Hoshino, S., Imai, M., Kobayashi, T., Uchida, N., Katada, T. 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA. Direct association of ERF3/GSPT with polyadenylate-binding protein. J. Biol. Chem. 274: 16677-16680.
64. Iizuka, N., Najita, L., Franzusoff, A. and Sarnow, P. 1994. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell Biol. 14: 7322-7330.
65. Imataka, H. and Sonenberg, N., 1997. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell Biol. 17: 6940-6947.
66. Imataka, H., Gradi, A. and Sonenberg, N. 1998. 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: 7480-7489.
67. James, P., Pfund, C. and Craig, E.A. 1997. Functional specificity among Hsp70 molecular chaperones. Science 275: 387-389.
68. Jaramillo, M., Dever, T.E., Merrick, W. C. and Sonenberg, N. 1991. RNA unwinding in translation: Assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B. Mol. Cell Biol. 11: 5992-5997.
69. Joshi, B., Yan, R. and Rhoads, R.E. 1994. In vitro synthesis of human protein synthesis initiation factor 4γ and its localization on 43 and 48 S initiation complexes. J. Biol. Chem. 269: 2048-2055.
70. Joshi, B., Cai, A.L., Keiper, B.D., Minich, W.B., Mendez, R., Beach, C.M., Stepinski, J., Stolarski, R., Darzynkiewicz, E. and Rhoads, R.E. 1995. Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209. J. Biol. Chem. 270: 14597-14603.
71. Joyce, G.F. 1999. Reactions catalyzed by RNA and DNA enzymes. In: The RNA World: The Nature of Modern RNA Suggests a Prebiotic RNA. 2nd Ed. Cold Spring Harbor, N.Y. Cold Spring Harbor Laboratory Press, 1999. Pp. 687-690.
72. Joyce, G.F. and Orgel, L.E. 1999. Prospects for understanding the origin of the RNA world. In: Gesteland, Raymond F., Cech, Thomas R., Atkins, John F. (eds), The RNA World: The Nature of Modern RNA Suggests a Prebiotic RNA. 2nd Ed. Cold Spring Harbor, N.Y. Cold Spring Harbor Laboratory Press, 1999. Pp. 49-77.
73. Kaufman, R.J. 2000. The double-stranded RNA-activated protein kinase PKR. In: Sonenberg, N., Hershey, J.W.B., Mathews, M.B. (eds.), Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp. 503-527.
74. Kessler, S.H. and Sachs, A.B. 1998. RNA recognition motif 2 of yeast Pablp is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell Biol. 18: 51-57.
75. Khaleghpour, K., Kahvejian, A., De Crescenzo, G., Roy, G., Svitkin, Y.V., Imataka, H., O'Connor-McCourt, M. and Sonenberg, N. 2001a. Dual interactions of the translational repressor Paip2 with poly(A) binding protein. Mol. Cell Biol. 21: 5200-5213.
76. Khaleghpour, K., Svitkin, Y.V, Craig, A.W., DeMaria, C.T., Deo, R.C., Burley, S.K. and Sonenberg, N. 2001b. Translational repression by a novel partner of human poly(A) binding protein, Paip2. Mol. Cell 7: 205-216.
77. Kim, C.Y., Takahashi, K., Nguyen, T.B., Roberts, J.K. and Webster, C. 1999. Identification of a nucleic acid binding domain in eukaryotic initiation factor eIFiso4G from wheat. J. Biol. Chem. 274: 10603-10608.
78. Korneeva, N.L., Lamphear, B.J., Hennigan, F.L. and Rhoads, R.E. 2000. Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J. Biol. Chem. 275: 41369-41376.
79. Korneeva, N.L., Lamphear, B.J., Hennigan, F.L., Merrick, W.C. and Rhoads, R.E. 2001. Characterization of the two eIF4A-binding sites on human elF4G-I. J. Biol. Chem. 276: 2872-2879.
80. Kozak, M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44: 283-292.
81. Kozlov, G., Trempe, J.F., Khaleghpour, K., Kahvejian, A., Ekiel, I., Gehring, K. 2001. Structure and function of the C-terminal PABC domain of human poly(A)-binding protein. Proc. Natl. Acad. Sci. USA 98: 4409-4413.
82. Kuhn, U, and Pieler, T. 1996. Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256: 20-30
83. Lamphear, B.J., Kirchweger, R., Skern, T. and Rhoads, R.E. 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases - Implications for cap-dependent and cap-independent translational initiation. J. Biol. Chem. 270: 21975-21983.
84. Langland, J.O., Jin, S., Jacobs, B.L. and Roth, D.A. 1995. Identification of a plant-encoded analog of PKR, the mammalian double-stranded RNA-dependent protein kinase. Plant Physiol. 108: 1259-1267.
85. Langland, J.O., Langland, L.A., Browning, K.S. and Roth, D.A. 1996. Phosphorylation of plant eukaryotic initiation factor-2 by the plant-encoded double-stranded RNA-dependent protein kinase, pPKR, and inhibition of protein synthesis in vitro. J. Biol. Chem. 271: 4539-4544.
86. Lawson, T.G., Lee, K.A., Maimone, M.M., Abramson, R.D., Dever, T.E., Merrick, W.C. and Thach R.E. 1989. Dissociation of double-stranded polynucleotide helical structures by eukaryotic initiation factors, as revealed by a novel assay. Biochem. 28: 4729-4734.
87. Lax, S., Fritz, W., Browning, K. and Ravel, J. 1985. Isolation and characterization of factors from wheat germ that exhibit eukaryotic initiation factor 4B activity and overcome 7-methylguanosine 5′-triphosphate inhibition of polypeptide synthesis. Proc. Natl. Acad. Sci. USA 82: 330-333.
88. Lax, S., Browning, K.S., Maia, D.M. and Ravel, J.M. 1986. ATPase activities of wheat germ initiation factors 4A, 4B, and 4F, J. Biol. Chem. 261: 15632-15636.
89. Le, H., Chang, S.-C., Tanguay, R.L. and Gallie, D.R. 1997a. The wheat poly(A)-binding protein functionally complements Pablp in yeast. Eur. J. Biochem. 243: 350-357.
90. Le, H., Tanguay, R.L., Balasta, M.L., Wei, C-C., Browning, K.S., Metz, A.M., Goss, D.J. and Gallie, D.R. 1997b. 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: 16247-16255
91. Le, H., Browning, K.S. and Gallie, D.R. 1998. The phosphorylation state of the wheat translation initiation factors eIF4B, eIF4A, and eIF2 is differentially regulated during seed development and germination. J. Biol. Chem. 273: 20084-20089
92. Le, H., Browning, K.S. and Gallie, D.R. 2000. The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B. J. Biol. Chem. 275: 17452-17462.
93. Li, W., Belsham, G.J., Proud, C.G. 2001. Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo. J. Biol. Chem. 276: 29111-29115.
94. Lin, T.-A., Kong, X., Haystead, T.A.J., Pause, A., Belsham, G., Sonenberg, N. and Lawrence, J.C. 1994. PHAS-I as a link between mitogen-activated protein kinase and translation initiation. Science 266: 653-656.
95. Ling, J., Wells, D.R., Tanguay, R.L., Dickey, L.F., Thompson, W.F. and Gallie, D.R. 2000. Heat shock protein HSP101 binds to the Fed-I internal light regulatory element and mediates its high translational activity. Plant Cell 12: 1213-1228.
96. Luo, Y. and Goss, D.J. 2001. Homeostasis in mRNA initiation: Wheat germ poly(A)-binding protein lowers the activation energy barrier to initiation complex formation. J. Biol. Chem. 276: 43083-43086.
97. Mader, S., Lee, H., Pause, A. and Sonenberg, N. 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol. Cell Biol. 15: 4990-4997.
98. Manzella, J.M., Rychlik, W., Rhoads R.E., Hershey, J.W. and Blackshear, P.J. 1991. Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eucaryotic initiation factors eIF-4B and eIF-4E. J. Biol. Chem. 266: 2383-2389.
99. Marcotrigiano, J., Gingras, A.C., Sonenberg, N. and Burley, S.K. 1997. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89: 951-961.
100. Marcotrigiano, J., Gingras, A.C., Sonenberg, N. and Burley, S.K. 1999. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 3: 707-716.
101. McKay, D.B. and Wedekind, J.E. 1999. In: Gesteland, Raymond F., Cech, Thomas R., Atkins, John F. (eds), Small Ribozymes. The RNA World: The Nature of Modern RNA Suggests a Prebiotic RNA. 2nd Ed. Cold Spring Harbor, N.Y. Cold Spring Harbor Laboratory Press, 1999. Pp. 265-286.
102. Methot, N., Song, M.S. and Sonenberg, N. 1996. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol. Cell Biol. 16: 5328-5334.
103. Metz, A.M. and Browning, K.S. 1997. Assignment of the β-subunit of wheat eIF2 by protein and DNA sequence analysis and immunoanalysis. Arch Biochem. Biophys. 342: 187-189.
104. Minich, W.B., Balasta, M.L., Goss, D.J. and Rhoads, R.E. 1994. Chromatographic resolution of in vivo phosphorylated and non-phosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91: 7668-72.
105. Muckenthaler, M., Gray, N.K. and Hentze, M.W. 1998. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Mol. Cell. 2: 383-388.
106. Naranda, T., MacMillan, S.E., Donahue, T.F. and Hershey, J.W. 1996. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell Biol. 16: 2307-2313.
107. Neff, C.L. and Sachs, A.B. 1999. Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally. Mol. Cell Biol. 19: 5557-5564.
108. Nelson, R.J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. and Craig, E.A. 1992. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71: 97-105.
109. Nissen, P., Hansen, J., Ban, N., Moore, P.B. and Steitz, T.A. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science 289: 920-930.
110. Otero, L.J., Ashe, M.P. and Sachs, A.B. 1999. The yeast poly(A)-binding protein Pablp stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBO J. 18: 3153-3163.
111. Pain, V.M. 1994. Translational control during amino acid starvation. Biochimie 76: 718-728.
112. Pain, V.M., 1996. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236: 747-771.
113. Palade, G. 1955. A Small particulate component of the cytoplasm. J. Biophys. Biochem. Cytol. 1: 59-67.
114. Palade, G. 1975. Intracellular aspects of the process of protein synthesis. Science 189: 347-358.
115. Park, H.S., Himmelbach, A., Browning, K.S., Hohn, T. and Ryabova, L.A. 2001. A plant viral 'reinitation' factor interacts with the host translational machinery. Cell 106: 723-733.
116. Pause, A., Belsham, G., Gingras, A.-C., Donze, O., Lin, T.-A., Lawrence, J.C. and Sonenberg, N. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371: 762-777.
117. Pestova, T.V., Shatsky, I.N. and Hellen, C.U. 1996. Functional dissection of eukaryotic initiation factor 4F: The 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43 S preinitiation complexes. Mol. Cell Biol. 16: 6870-6878.
118. Pestova, T.V., Borukhov, S.I. and Hellen, C.U. 1998. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 394: 854-859.
119. Petracek, M.E., Dickey, L.F., Nguyen, T.-T, Gatz, C., Sowinski, D.A., Allen, G.C. and Thompson, W.F. 1998. Ferredoxin-1 mRNA is destabilized by changes in photosynthetic electron transport. Proc. Natl. Acad. Sci. USA 95: 9009-9013.
120. Pfund, C., Lopez-Hoyo, N., Ziegelhoffer, T., Schilke, B.A., Lopez-Buesa, P., Walter, W.A., Wiedmann, M. and Craig, E.A. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17: 3981-3989.
121. Phan, L., Zhang, X.L., Asano, K., Anderson, J., Vornlocher, H.P., Greenberg, J.R., Qin, J. and Hinnebusch, A.G. 1998. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell Biol. 18: 4935-4946.
122. Piron, M., Vende, P., Cohen, J. and Poncet, D. 1998. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. EMBO J. 17: 5811-5821.
123. Piron, M., Delaunay, T., Grosclaude, J. and Poncet, D. 1999. Identification of the RNA-binding, dimerization, and eIF4GI-binding domains of rotavirus nonstructural protein NSP3. J. Virol. 73: 5411-5421.
124. Poncet, D., Aponte, C. and Cohen, J. 1993. Rotavirus protein NSP3 (NS34) is bound to thc 3′ end consensus sequence of viral mRNAs in infected cells. J. Virol. 67: 3159-3165.
125. Poulin, F., Gingras, A.C., Olsen, H., Chevalier, S. and Sonenberg, N. 1998. 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family. J. Biol. Chem. 273: 14002-14007.
126. Pyronnet, S., Imataka, H., Gingras, A.C., Fukunaga, R., Hunter, T. and Sonenberg, N. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J. 18: 270-279.
127. Raught, B., Gingras, A.-C., Gygi, S.P., Imataka, H., Morino, S., Gradi, A., Aebersold, R. and Sonenberg, N. 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19: 434-444.
128. Ray, B.K., Lawson, T.G., Kramer, J.C., Cladaras, M.H., Grifo, J.A., Abramson, R.D., Merrick, W.C. and Thach, R.E. 1985. ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors. J. Biol. Chem. 260: 7651-7658.
129. Rochaix, J.D. 1996. Post-transcriptional regulation of chloroplast gene expression in Chlamydomonas reinhardtii. Plant Mol. Biol. 32: 327-341.
130. Ron, D. and Harding, H.P. 2000. PERK and translational control by stress in the endoplasmic reticulum. In: Sonenberg, N., Hershey, J.W.B. and Mathews, M.B. (eds), Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp. 547-560.
131. Rouault, T.A. and Harford, J.B. 2000. Translational control of ferritin synthesis. In: Sonenberg, N., Hershey, J.W.B., Mathews, M.B. (eds), Translational Control of Gene Expression, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Pp, 655-670.
132. Rozen, F., Edery, I., Meerovitch, K., Dever, T.E., Merrick, W.C. and Sonenberg, N. 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell Biol. 10: 1134-1144.
133. Sachs, A.B., Davis, R.W. and Kornberg, R.D. 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
134. Scheper, G.C., van Kollenburg, B., Hu, J., Luo, Y., Goss, D.J. and Proud, C.G. 2001. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem., in press.
135. Scholthof, H.B., Gowda, S., Wu, F.C. and Shepherd, R.J. 1992. The full-length transcript of a caulimovirus is a polycistronic mRNA whose genes are trans activated by the product of gene VI. J. Virol. 66: 3131-3139.
136. Schuler, G.D., Altschul, S.F. and Lipman, D.J. 1991. A workbench for multiple alignment construction and analysis. Proteins 9: 180-190.
137. Smith, B.L., Gallie, D.R., Le, H. and Hansma, P.K. 1997. Visualization of poly(A)-binding protein complex formation with poly(A) RNA using atomic force microscopy. J. Struc. Biol. 119: 109-117.
138. Somanchi, A., Mayfield, S.P. 1999. Nuclear-chloroplast signalling. Curr. Opin. Plant Biol. 2: 404-409.
139. Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth. In: Translational Control, Hershey, J.W.B., Mathews, M. B., and Sonenberg, N. eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. pp. 249-269.
140. Stambuk, R.A. and Moon, R.T. 1992. Purification and characterization of recombinant Xenopus poly(A)(+)-binding protein expressed in a baculovirus system. Biochem. J. 287: 761-766.
141. Tarun, S.Z. and Sachs, A.B. 1995. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Devel. 9: 2997-3007.
142. Tarun, S.Z. and Sachs, A.B. 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15: 7168-7177.
143. Tarun, S.Z., Wells, S.E., Deardorff, J.A. and Sachs, A.B. 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94: 9046-9051.
144. Vende, P., Piron, M., Castagne, N. and Poncet, D. 2000. Efficient translation of rotavirus mRNA requires simultaneous interaction of NSP3 with the eukaryotic translation initiation factor eIF4G and the mRNA 3′ end. J. Virol. 74: 7064-7071.
145. Vornlocher, H.P., Hanachi, P., Ribeiro, S., Hershey, J.W. 1999. A 110-kilodalton subunit of translation initiation factor eIF3 and an associated 135-kilodalton protein are encoded by the Saccharomyces cerevisiae TIF32 and TIF3I genes. J. Biol. Chem. 274: 16802-16812.
146. Wei, C-C., Balasta, M.L., Ren, J. and Goss, D.J. 1998. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues. Biochem. 37: 1910-1916.
147. Wek, R.C. 1994. eIF-2 kinases: Regulators of general and gene specific translation initiation. Trends Biochem. Sci. 19: 491-496.
148. Wells, D.R., Tanguay, R.L., Le, H. and Gallie, D.R. 1998a. HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Devel. 12: 3236-3251.
149. Wells, S.E., Hillner, P.E., Vale, R.D. and Sachs, A.B. 1998b. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2: 135-140
150. Zelus, B.D., Giebelhaus, D.H., Eib, D.W., Kenner, K.A. and Moon, R.T. 1989. Expression of the poly(A)-binding protein during development of Xenopus laevis. Mol. Cell Biol. 9: 2756-2760.
151. Zhong, T. and Arndt, K.T. 1993. The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73: 1175-1186.