Moonlighting functions of polypeptide elongation factor 1: From actin bundling to zinc finger protein R1-associated nuclear localization

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 1, 2002, Pages 1-21

  Ejiri, Shin Ichiro ^a  

^a IWATE UNIVERSITY   (Japan)

Author keywords

Apoptosis; Cancer; Elongation factor 1; Protein biosynthesis; Translation

Indexed keywords

ANIMALIA; EUKARYOTA;

ACTIN; CARRIER PROTEIN; CYSTEINE PROTEINASE; ELONGATION FACTOR 1; MULTIENZYME COMPLEX; PEPTIDE; PROTEASOME; PROTEIN DISULFIDE ISOMERASE; SELENOCYSTEINE; ZINC FINGER PROTEIN; ZNF259 PROTEIN, HUMAN;

ANIMAL; APOPTOSIS; CELL NUCLEUS; COLD; CYTOSKELETON; GENETICS; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; METABOLISM; MOLECULAR MIMICRY; PHYSIOLOGY; PROTEIN SYNTHESIS; REVIEW; SIGNAL TRANSDUCTION; WEST NILE FLAVIVIRUS;

ACTINS; ANIMALS; APOPTOSIS; CARRIER PROTEINS; CELL NUCLEUS; COLD; CYSTEINE ENDOPEPTIDASES; CYTOSKELETON; HERPESVIRUS 1, HUMAN; HIV-1; HUMANS; MOLECULAR MIMICRY; MULTIENZYME COMPLEXES; PEPTIDE ELONGATION FACTOR 1; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BIOSYNTHESIS; PROTEIN DISULFIDE-ISOMERASE; SELENOCYSTEINE; SIGNAL TRANSDUCTION; WEST NILE VIRUS; ZINC FINGERS;

EID: 0036359281     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1     Document Type: Article

References (176)

1. Zamecnik, P. C., An historical account of protein synthesis, with current overtones—a personalized view. In “Symposia on quantitative biology: The mechanism of protein synthesis”, Univ. of Tokyo Press, Tokyo, 34, 1-16 (1969).
2. Fessenden, J. M. and Moldave, K., Studies on amino acyl transfer from soluble RNA to ribosomes; resolution of two soluble transferring activities. J. Biol. Chem., 238, 1479-1484 (1963).
3. Nishizuka, Y. and Lipmann, F., Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system. Proc. Natl. Acad. Sci. USA, 55, 212-219 (1966).
4. Lucas-Lenard, J. and Lipmann, F., Separation of three microbial amino acid polymerization factors. Proc. Natl. Acad. Sci. USA, 55, 1562-1566 (1966).
5. Weissbach, H., Miller, D. L., and Hachmann, J., Studies on the role of factor Ts in polypeptide synthesis. Arch. Biochem. Biophys., 137, 262-269 (1970).
6. Galasinski, W. and Moldave, K., Purification of aminoacyltransferase II (translocation factor) from rat liver. J. Biol. Chem., 244, 6527-6532 (1969).
7. Taira, H., Ejiri, S., and Shimura, K., Purification and some properties of G-factor from the silk gland of silkworm. J. Biochem., 72, 1527-1535 (1972).
8. McKeehan, W. L. and Hardesty, B., Purification and partial characterization of the aminoacyl transfer ribonucleic acid binding enzyme from rabbit reticulocytes. J. Biol. Chem., 244, 4330-4339 (1969).
9. Moon, H. M., Redfield, B., Millard, S., Vane, F., and Weissbach, H., Multiple forms of elongation factor 1 from calf brain. Proc. Natl. Acad. Sci. USA, 70, 3282-3286 (1973).
10. Ejiri, S., Murakami, K., and Katsumata, T., Elongation factor 1 from the silk gland of silkworm. Purification and some properties of its g subunit having EF-1β activity. FEBS Lett., 8, 111-114 (1977).
11. Ejiri, S., Purification and characterization of polypeptide chain elongation factor 1 from plants. Methods Enzymol., Academic Press, Orlando, 118, 140-153 (1986).
12. Janssen, G. M. C., Damme, H. T. F. v., Kriek, J., Amons, R., and Möller, W., The subunit structure of elongation factor 1 from Artemia: Why two unchains in this complex? J. Biol. Chem., 269, 31410-31417 (1994).
13. Miyazaki, M., Uritani, M., Fujimura, K., Yamakatsu, H., Kageyama, T., and Takahashi, K., Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1α and 1β (γ) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe. J. Biochem., 103, 508-521 (1988).
14. Uritani, M. and Miyazaki, M., Role of yeast peptide elongation factor 3 (EF-3) at the AA-tRNA binding step. J. Biochem., 104, 118-126 (1988).
15. Chakraburtty, K., Functional interaction of yeast elongation factor 3 with yeast ribosomes. Int. J. Biochem. Cell Biol., 31, 163-173 (1999).
16. Jeffery, C. J., Moonlighting proteins. TIBS, 24, 8-11 (1999).
17. Noller, H. F., Green, R., Heilek, G., Hoffarth, V., Huttenhofer, A., Joseph, S., Lee, I., Lieberman, K., Mankin, A., and Merryman, C., Structure and function of ribosomal RNA. Biochem. Cell Biol., 73, 997-1009 (1995).
18. Al-Karadaghi, S., Kristensen, O., and Liljas, A., A decade of progress in understanding the structural basis of protein synthesis. Prog. Biophys. Mol. Biol., 73, 167-193 (2000).
19. Nierhaus, K. H., Stuhrmann, H. B., and Svergun, D., The ribosomal elongation cycle and the movement of tRNAs across the ribosome. Prog. Nucleic AcidRes. Mol. Biol., 59, 177-204 (1998).
20. Phe, EF-Tu, and a GTP analog. Science, 270, 1464-1472 (1995).
21. Kim, K. K., Min, K., and Suh, S. W., Crystal structure of the ribosome recycling factor from Escherichia coli. EMBO J., 19, 2362-2370 (2000).
22. Nakamura, Y., Ito, K., and Ehrenberg, M., Mimicry grasps reality in translation termination. Cell, 101, 349-352 (2000).
23. Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A., and Liljas, A., Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic. Science, 286, 2349-2352 (1999).
24. Condeelis, J., Elongation factor 1a, translation and the cytoskeleton. TIBS, 20, 169-170 (1995).
25. Kidou, S. and Ejiri, S., Isolation, characterization and mRNA expression of four cDNAs encoding translation elongation factor 1A from rice (Oryza sativa L.). Plant Mol. Biol., 36, 137-148 (1998).
26. Iwabe, N., Kuma, K., Hasegawa, M., Osawa, S., and Miyata, T., Evolutionary relationship of ar-chaebacteria, eubacteria and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc. Natl. Acad. Sci. USA, 86, 9355-9359 (1989).
27. Frydenberg, J., Poulsen, K., Petersen, A. K., Lund, A., and Olesen, O. F., Isolation and characterization of the gene encoding EF-1a O, an elongation factor 1-a expressed during early development of Xenopus laevis. Gene, 109, 185-192 (1991).
28. Axelos, M., Bardet, C., Liboz, T., Thai, A. L. V., Curie, C., and Lescure, B., The gene family encoding the Arabidopsis thaliana translation elongation factor EF-1α: Molecular cloning, characterization and expression. Mol. Gen. Genet., 219, 106-112 (1989).
29. Manevski, A., Bertoni, G., Bardet, C., Tremousaygue, D., and Lescure, B., In synergy with various cis-acting elements, plant insterstitial telomere motifs regulate gene expression in Arabidopsis root meristems. FEBS Lett., 483, 43-46 (2000).
30. Sprang, S. R., G protein mechanisms: Insights from structural analysis. Annu. Rev. Biochem., 66, 639-678 (1997).
31. Sprinzl, M., Elongation factor Tu: a regulatory GTPase with an integrated effector. TIBS, 19, 245-250 (1994).
32. Terui, Y., Tsutsumi, K., Kidou, S., Sawazaki, T., Kuroiwa, Y., Yamaki, M., and Ejiri, S., A novel variant of translation elongation factor-1β: isolation and characterization of the rice gene encoding EF-1β2. Biochimi. Biophysi. Acta, 1442, 369-372 (1998).
33. Kawashima, T., Berthet-Colominas, G., Wulff, M., Cusack, S., and Leberman, R., The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution. Nature, 379, 511-518 (1996).
34. Ejiri, S., Kawamura, R., and Katsumata, T., Interaction among four elongation factor 1 from rice subunits of embryos. Biochim. Biophys. Acta, 1217, 266-272 (1994).
35. Perez, J. M. J., Siegal, G., Kriek, J., Hard, K., Dijk, J., Canters, G. W., and Möller, W., The solution structure of the guanine nucleotide exchange domain of human elongation factor 1b reveals a striking resemblance to that of EF-Ts from Escherichia coli. Structure, 7, 217-226 (1999).
36. Kamiie, K., Taira, H., Kobayashi, K., Yamashita, T., Kidou, S., and Ejiri, S., Expression of elongation factor 1β' in Escherichia coli and its interaction with elongation factor 1a from silk gland. Biosci. Biotechnol. Biochem., 63, 666-671 (1999).
37. Janssen, G. M., and Moller, W., Elongation factor 1bg from Artemia. Purification and properties of its subunits. Eur. J. Biochem., 171, 119-129 (1988).
38. Koonin, E. V., Mushegian, A. R., Tatusov, R. L., Altschul, S. F., Bryant, S. H., Bork, P., and Valencia, A., Eukaryotic translation elongation factor 1γ contains a glutathione transferase domain-study of a diverse, ancient protein superfamily using motif search and structural modeling. Protein Sci., 3, 2045-2054 (1994).
39. Kanaoka, Y., Ago, H., Inagaki, E., Nanayama, T., Miyano, M., Kikuno, R., Fujii, Y., Eguchi, N., Toh, H., Urade, Y., and Hayashi, O., Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell, 90, 1085-1095 (1997).
40. Marrs, K. A., Alfenito, M. R., Lloyd, A. M., and Walbot, V., A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2. Nature, 375, 397-400 (1995).
41. Plumas-Marty, B., Verwaerde, C., Loyens, M., Velge, P., Taibi, A., Cesbron, M.-F., Capron, A., and Ouaissi, M. A., Trypanosoma cruziglutathione-binding proteins: immunogenicity during human and experimental Chagas’ disease. Parasitology, 104, 87-98 (1992).
42. Quevillon, S. and Mirande, M., The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1. FEBS Lett., 395, 63-67 (1996).
43. Negrutskii, B. S., Shalak, V. F., Kerjan, P., El’skaya, A. V., and Mirande, M., Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1α in the complex with EF-1H. J. Biol. Chem., 274, 4545-4550 (1999).
44. Negrutskii, B. S. and El’skaya, A. V., Eukaryotic translation elongation factor 1a: structure, expression, functions, and possible role in aminoacyl-tR-NA channeling. Prog. Nucleic Acid Res. Mol. Biol., 60, 47-78 (1998).
45. Stapulionis, R., Kolli, S., and Deutscher, M. P., Efficient mammalian protein synthesis requires an intact F-actin system. J. Biol. Chem., 272, 24980-24986 (1997).
46. Sonenberg, N., Hershey, J. W. B., and Mathews, M. B., In “Translational control of gene expression”, Cold Spring Harbor Laboratory Press, New York (2000).
47. Kielbassa, K., Muller, H. J., Meyer, H. E., Marks, F., and Gschwendt, M., Protein kinase C δ-specific phosphorylation of the elongation factor eEF-α and an eEF-1α peptide at threonine 431. J. Biol. Chem., 270, 6156-6162 (1995).
48. Anvi, D., Biberman, Y., and Meyuhas, O., The 5’ terminal oligpyrimidine tract confers translational control on TOP mRNAs in a cell type- and sequence context-dependent manner. Nucl. Acids Res., 25, 995-1001 (1997).
49. Janssen, G. M., Morales, J., Schipper, A., Labbe, J. C., Mulner-Lorillon, O., Belle, R., and Möller, W., A major substrate of maturation promoting factor identified as elongation factor 1βγδ in Xenopus laevis. J. Biol. Chem., 266, 14885-14888 (1991).
50. Wang, L., Wang, X., and Proud, C. G., Activation of mRNA in rat cardiac myocytes by insulin involves multiple rapamycin-sensitive steps. Am J. Physiol. Heart Circ. Physiol., 278, H1056-1068 (2000).
51. Everett, A. D., Stoops, T. D., Nairn, A. C., and Brautigan, D., Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. Am J. Physiol. Heart Circ. Physiol., 281, H161-167 (2001).
52. s6k. EMBO J., 16, 3693-3704 (1997).
53. Chang, Y.-W. E. and Traugh, J. A., Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation. J. Biol. Chem., 272, 28252-28257 (1997).
54. Kimball, S. R., Shantz, L. M., Horetsky, R. L., and Jefferson, L. S., Leucine regulates translation of specific mRNAs in L6 myoblasts through mTOR-mediated changes in availability of eIF4E and phosphorylation of ribosomal protein S6. J. Biol. Chem., 274, 11647-11652 (1999).
55. Montagne, J., Stewart, M. J., Stocker, H., Hafen, E., Kozma, S. C., and Thomas, G., Drosophila S6 kinase: A regulator of cell size. Science, 285, 2126-2129 (1999).
56. Whiteheart, S. W., Shenbagamurthi, P., Chen, L., Cotter, R. J., and Hart, G. W., Murine elongation factor 1α (EF-1α) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phospho-glycerol to specific glutamic acid residues on EF-1α. J. Biol. Chem., 264, 14334-14341 (1989).
57. Hayashi, Y., Urade, R., Utsumi, S., and Kito, M., Anchoring of peptide elongation factor EF-1α by phosphatidylinositol at the endoplasmic reticulum membrane. J. Biochem., 106, 560-563 (1989).
58. Kraal, B., Lippmann, C., and Kleanthous, C., Translational regulation by modifications of the elongation factor Tu. Folia. Microbiol., 44, 131-141 (1999).
59. Zobel-Thropp, P., Yang, M. C., Machado, L., and Clarke, S., A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus. J. Biol. Chem., 275, 37150-37158 (2000).
60. Fruman, D. A., Meyers, R. E., and Cantley, L. C., Phosphoinositide kinases. Annu. Rev. Biochem., 67, 481-507 (1998).
61. Yang, W., Burkhart, W., Cavallius, J., Merrick, W. C., and Boss, W. F., Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells. J. Biol. Chem., 268, 392-398 (1993).
62. Yang, W. and Boss, W. F., Regulation of phos-phatidylinositol 4-kinase by the protein activator PIK-A49. J. Biol. Chem., 269, 3852-3857 (1994).
63. Kim, M. J., Si, F., Kim, S. J., Hong, S. B., Hwang, J. I., Lee, H. J., Lee, S. J., Chang, J. S., Lee, Y. H., Ryu, S. H., and Suh, P. G., The SH2-SH2-SH3 domain of phospholipase C-γ1 directly binds to translational elongation factor-1a. Mol. Cells, 9, 631-637 (1999).
64. Wang, W. and Poovaiah, B. W., Interaction of plant chimeric calcium/calmodulin-dependent protein kinase with a homolog of eukaryotic elongation factor-1α. J. Biol. Chem., 274, 12001-12008 (1999).
65. 2+/calmodulin. J. Biochem., 119, 791-798 (1996).
66. Ransom-Hodgkins, W. D., Breglez, I., Wang, X., and Boss, W. F., Calcium-regulated proteolysis of eEF1A. Plant Physiol., 122, 957-965 (2000).
67. Amano, S., Kawasaki, H., Ishiura, S., Kawashima, S., Suzuki, K., and Emori, Y., Identification of endogenous substrates for Drosophila calpain from a salt-extracted fraction of Drosophila ovaries. J. Biochem., 122, 865-871 (1997).
68. Redpath, N. T., Foulstone, E. J., and Proud, C. G., Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway. EMBO J., 15, 2291-2297 (1996).
69. Redpath, N. T. and Proud, C. G., The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2. Biochem. J., 262, 69-75 (1989).
70. Bell, C. E., Poon, P. H., Schumaker, V. N., and Eisenberg, D., Oligomerization of a 45 kilodalton fragment of diphtheria toxin at pH 5.0 to a molecule of 20-24 subunits. Biochemistry, 36, 15201-15207 (1997).
71. Honjo, T. and Hayaishi, O., Enzymatic ADP-ribosylation of proteins and regulation of cellular activity. Curr. Top. Cell Regul., 7, 87-127 (1973).
72. Fendrick, J. L., Iglewski, W. J., Moehring, J. M., and Moehring, T. J., Characterization of the endogenous ADP-ribosylation of wild-type and mutant elongation factor 2 in eukaryotic cells. Eur. J. Biochem., 205, 25-31 (1992).
73. Falnes, P. O., Ariansen, S., Sandvig, K., and Olsnes, S., Requirement for prolonged action in the cytosol for optimal protein synthesis inhibition by diphtheria toxin. J. Biol. Chem., 275, 4363-4368 (2000).
74. Kimata, Y. and Kohno, K., Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth. J. Biol. Chem., 269, 13497-13501 (1994).
75. Nishioka, K., Atopic eczema of adult type in Japan. Australasian J. Dermatol., 37, S7-S9 (1996).
76. Ohkouchi, K., Mizutani, H., Tanaka, M., Takahashi, M., Nakashima, K., and Shimizu, M., Anti-elongation factor-1a autoantibody in adult atopic dermatitis patients. Int. Immunol., 11, 1635-1640 (1999).
77. Alberdi, F., Dadone, J., Ryazanov, A., Isenberg, D. A., and Reichlin, M., Cross-reaction of lupus antidsDNA antibodies with protein translation factor EF-2. Clin. Immunol., 98, 293-300 (2001).
78. Ditzel, H. J., Masaki, Y., Nielsen, H., Farnaes, L., and Burton, D. R., Cloning and expression of a novel human antibody-antigen pair associated with Felty’s syndrome. Proc. Natl. Acad. Sci. USA, 97, 9234-9239 (2000).
79. Uchiumi, T., Traut, R. R., Elkon, K., and Kominami, R., A human autoantibody specific for a unique conserved region of 28 S ribosomal RNA inhibits the interaction of elongation factors 1a and 2 with ribosomes. J. Biol. Chem., 266, 2054-2062 (1991).
80. Steiner, G., Skriner, K., and Smolen, J. S., Autoanitibodies to the A/B proteins of the heterogeneous nuclear ribonucleoprotein complex: novel tools for the diagnosis of rheumatic diseases. Int. Arch. Allergy Immunol., 111, 314-319 (1996).
81. Ligier, S., Fortin, P. R., and Newkirk, M. M., A new antibody in rheumatoid arthritis targeting glycated IgG: IgM anti-IgG-AGE. Br. J. Rheumatol., 37, 1307-1314 (1998).
82. Johnson, G., Gotlib, J., Haroutunian, V., Bierer, L., Nairn, A. C., Merril, C., and Wallace, W., Increased phosphorylation of elongation factor 2 in Alzheimer’s disease. Brain Res. Mol. Brain Res., 15, 319-326 (1992).
83. Langstrom, N. S., Anderson, J. P., Lindroos, H. G., Winblad, B., and Wallace, W. C., Alzheimer’s disease-associated reduction of polysomal mRNA translation. Brain. Res. Mol. Brain Res., 5, 259-269 (1989).
84. Reynet, C. and Kahn, C. R., Unbalanced expression of the different subunits of elongation factor 1 in diabetic skeletal muscle. Proc. Natl. Acad. Sci. USA, 98, 3422-3427 (2001).
85. Vary, T. C., Nairn, A., and Lynch, C. J., Role of elongation factor 2 in regulating peptide-chain elongation in the heart. Am. J. Physiol., 266, E628-E634 (1994).
86. Grant, A. G., Flomen, R. M., Tizard, M. L., and Grant, D. A., Differential screening of a human pancreatic adenocarcinoma λgt11 expression library has identified increased transcription of elongation factor EF-1α in tumour cells. Int. J. Cancer, 50, 740-745 (1992).
87. Edmonds, B. T., Wyckoff, J., Yeung, Y.-G., Wang, Y., Stanley, E. R., Jones, J., Segall, J., and Condee-lis, J., Elongation factor-1α is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma. J. Cell Sci., 109, 2705-2714 (1996).
88. Frazier, M. L., Inamdar, N., Alvula, S., Wu, E., and Kim, Y. H., Few point mutations in elongation factor-1γ gene in gastrointestinal carcinoma. Mol. Carcinog., 22, 9-15 (1998).
89. Chi, K., Jones, D. V., and Frazier, M. L., Expression of an elongation factor 1g-related sequence in adenocarcinomas of the colon. Gastroenterlogy, 103, 98-102 (1992).
90. Mathur, S., Cleary, K. R., Inamdar, N., Kim, Y. H., Steck, P., and Frazier, M. L., Overexpression of elongation factor-1γ protein in colorectal carcinoma. Cancer, 82, 816-821 (1998).
91. Kolettas, E., Lymboura, M., Khazaie, K., and Luqmani, Y., Modulation of elongation factor-1δ (EF-1δ) expression by oncogenes in human epithelial cells. Anticancer Res., 18, 385-392 (1998).
92. Tatsuka, M., Mitsui, H., Wada, M., Nagata, A., Nojima, H., and Okayama, H., Elongation factor-1α gene determines susceptibility to transformation. Nature, 359, 333-336 (1992).
93. Su, Z.-Z., Goldstein, N. I., and Fisher, P. B., Antisense inhibition of the PTI-1 oncogene reverses cancer phenotypes. Proc. Natl. Acad. Sci. USA, 95, 1764-1769 (1998).
94. Gopalkrishnan, R. V., Su, Z. Z., Goldstein, N. I., and Fisher, P. B., Translational infidelity and human cancer: role of the PTI-1 oncogene. Int. J. Biochem. Cell Biol., 31, 151-162 (1999).
95. Talukder, A. H., Jorgensen, H. F., Mandal, M., Mishra, S. K., Vadlamudi, R. K., Clark, B. F. C., Mendelsohn, J., and Kumar, R., Regulation of elon-gataion factor-1α expression by growth factors and anti-receptor blocking antibodies. J. Biol. Chem., 276, 5636-5642 (2001).
96. Clemens, M. J. and Bommer, U.-A., Translational control: the cancer connection. Int. J. Biochem. Cell Biol., 31, 1-23 (1999).
97. Billaut-Mulot, O., Fernadez-Gomez, R., Loyens, M., and Ouaissi, A., Trypanosoma cruzi elongation factor 1-α: nuclear localization in parasites undergoing apoptosis. Gene, 174, 19-26 (1996).
98. Xiao, H., Neuveut, C., Benkirane, M., and Jeang, K.-T., Interaction of the second coding exon of Tat with human EF-1d delineates a mechanism for HIV-1-mediated shutoff of host mRNA translation. Biochem. Biophys. Res. Commun., 244, 384-389 (1998).
99. Harsdorf, R. v., Li, P.-F., and Dietz, R., Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis. Circulation, 99, 2934-2941 (1999).
100. Kato, M. V., Sato, H., Nagayoshi, M., and Ikawa, Y., Upregulation of the elongation factor-1α gene by p53 in association with death of an erythroleukemic cell line. Blood, 90, 1373-1378 (1997).
101. Kato, M. V., The mechanisms of death of an erythroleukemic cell line by p53: involvement of the microtubule and mitochondria. Leuk. Lymphoma., 33, 181-186 (1999).
102. Duttaroy, A., Bourbeau, D., Wang, X.-L., and Wang, E., Apoptosis rate can be accelerated or decelerated by overexpression of reduction of the level of elongation factor-1α. Exp. Cell Res., 238, 168-176 (1998).
103. Chen, E., Proestou, G., Bourbeau, D., and Wang, E., Rapid up-regulation of peptide elongation factor EF-1a protein levels is an immediate early event during oxidative stress-induced apoptosis. Exp. Cell Res., 259, 140-148 (2000).
104. Matsuzawa, A. and Ichijo, H., Molecular mechanisms of the decision between life and death: Regulation of apoptosis by apoptosis signal-regulating kinase 1. J. Biochem., 130, 1-8 (2001).
105. Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S., A caspase-activated DNase that degrades DNA during apopto-sis, and its inhibitor ICAD. Nature, 391, 43-50 (1998).
106. Welle, S., Thornton, C., Bhatt, K., and Krym, M., Expression of elongation factor-1α and S1 in young and old human skeletal muscle. J. Gerontol. A Biol. Sci. Med. Sci., 52, B235-B239 (1997).
107. Shepherd, J. C., Walldorf, U., Hug, P., and Gehrin, W. J., Fruit flies with additional expression of the elongation factor EF-1α live longer. Proc. Natl. Acad. Sci. USA, 86, 7520-7521 (1989).
108. Stearns, S. C. and Kaiser, M., The effects of enhanced expression of elongation factor EF-1α on lifespan in Drosophila melanogaster. IV. A summary of three experiments. Genetica, 91, 167-182 (1993).
109. Gems, D., Sutton, A. J., Sundermeyer, M. L., Albert, P. S., King, K. V., Edgley, M. L., Larsen, P. L., and Riddle, D. L., Two pleiotropic classes of daf-2 mutation affect larval arrest, adult behavior, reproduction and longevity in Caenorhabditis ele-gans. Genetics, 150, 129-155 (1998).
110. Kimura, K. D., Tissenbaum, H. A., Liu, Y., and Ruvkun, G., daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science, 277, 942-946 (1997).
111. Blumenthal, T. and Carmichael, G. G., RNA replication: function and structure of Qb-replicase. Ann. Rev. Biochem., 48, 525-548 (1979).
112. Das, T., Mathur, M., Gupta, A. K., Janssen, G. M. C., and Banerjee, A. K., RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1abg for its activity. Proc. Natl. Acad. Sci. USA, 95, 1449-1454 (1998).
113. Blackwell, J. L. and Brinton, M. A., Translation elongation factor-1a interacts with the 3? stem-loop region of West Nile virus genomic RNA. J. Virol., 71, 6433-6444 (1997).
114. You, S. and Padmanabhan, R., A novel in vitro replication system for Dengue virus. Initiation of RNA synthesis at the 3’-end of exogenous viral RNA templates requires 5’- and 3’-terminal complementary sequence motifs of the viral RNA. J. Biol. Chem., 274, 33714-33722 (1999).
115. Dreher, T. W., Uhlenbeck, O. C., and Browning, K. S., Quantitative assessment of EF-1a. GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu. J. Biol. Chem., 274, 666-672 (1999).
116. Barton, D. J., O’Donnell, B. J., and Flanegan, J. B., 5’ cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis. EMBO J., 20, 1439-1448 (2001).
117. Cimarelli, A. and Luban, J., Translation elongation factor 1-α interacts specifically with the human immunodeficiency virus type 1 gag polyprotein. J. Virol., 73, 5388-5401 (1999).
118. Liu, B., Dai, R., Tian, C. J., Dawson, L., Gorelick, R., and Yu, X. F., Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin. J. Virol., 73, 2901-2908 (1999).
119. Roizman, B., HSV gene functions: what have we learned that could be generally applicable to its near and distant cousins? Acta Virol., 43, 75-80 (1999).
120. Kawaguchi, Y., Matsumura, T., Roizman, B., and Hirai, K., Cellular elongation factor 1δ is modified in cells infected with representative α-, β-, or γ herpesviruses. J. Virol., 73, 4456-4460 (1999).
121. Benard, L., Carroll, K., Valle, R. C. P., Masison, D. C., and Wickner, R. B., The Ski7 antiviral protein is an EF1-α homolog that blocks expression of non-poly(A) mRNA in Saccharomyces cerevisiae. J. Virol., 73, 2893-2900 (1999).
122. Dunn, M. A., Morris, A., Jack, P. L., and Hughes, M. A., A low-temperature-responsive translation elongation factor 1a from barley (Hordeum vulgare L.). Plant Mol. Biol., 23, 221-225 (1993).
123. Silar, P. and Picard, M., Increased longevity of EF-1α high-fidelity mutants in Podospora anserina. J. Mol. Biol., 235, 231-236 (1994).
124. Browning, K. S., The plant translational apparatus. Plant Mol. Biol., 32, 107-144 (1996).
125. Berberich, T., Sugawara, K., Harada, M., and Kusano, T., Molecular cloning, characterization and expression of an elongation factor 1a gene in maize. Plant Mol. Biol., 29, 611-615 (1995).
126. Simon, E., Effect of acclimation temperature on the elongation step of protein synthesis in different organs of rainbow trout. J. Comp. Physiol., 157, 201-207 (1987).
127. Haschemeyer, A. E., and Rappaport, S., Hybrid protein synthetic systems: components required to confer poikilothermy to the mammal. Comp Biochem Physiol B, 81, 705-709 (1985).
128. Berchet, V., Thomas, T., Cavicchioli, R., Russell, N. J., and Gounot, A. M., Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis SI55. Extremophiles, 4, 123-130 (2000).
129. Ripmaster, T. L., Vaughn, G. P., and Woolford, J. L., DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 7901-7912 (1993).
130. Kuriyama, R., Savereide, P., Lefebvre, P., and Dasgupta, S., The predicted amino acid sequence of a centrosphere protein in dividing sea urchin eggs is similar to elongation factor (EF-1α). J. Cell Sci., 95, 231-236 (1990).
131. Bassell, G. J., Powers, C. M., Taneja, K. L., and Singer, R. H., Single mRNAs visualized by ultras-tructural in situ hybridization are principally localized at actin filament intersections in fibroblasts. J. Cell Biol., 126, 863-876 (1994).
132. Yang, F., Demma, M., Warren, V., Dharmawardhane, S., and Condeelis, J., Identifica-ton of an actin-binding protein from Dictyostelium as elongation factor 1α. Nature, 347, 494-496 (1990).
133. Kurasawa, Y., Watanabe, Y., and Numata, O., Characterization of F-actin bundling activity of Tetrahymena elongation factor 1a investigated with rabbit skeletal muscle actin. Zoolog. Sci., 13, 371-375 (1996).
134. Bektas, M., Nurten, R., Gurel, Z., Sayers, Z., and Bermek, E., Interaction of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. FEBS Lett., 356, 89-93 (1994).
135. Morelli, J. K., Shewmaker, C. K., and Vayda, M. E., Biphasic stimulation of translational activity correlates with induction of translation elongation factor 1 subunit a upon wounding in potato tubers. Plant Physiol., 106, 897-903 (1994).
136. Zhu, J.-K., Damsz, B., Kononowicz, A. K., A. R. Bressan, and Hasegawa, P. M., A higher plant extracellular vitronectin-like adhesion protein is related to the translational elongation factor-1α. Plant Cell, 6, 393-404 (1994).
137. Shiina, N., Gotoh, Y., Kubomura, N., Iwamatsu, A., and Nishida, E., Microtubule severing by elongation factor 1α. Science, 266, 282-285 (1994).
138. Durso, N. A. and Cyr, R. J., A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongaton factor-1α. Plant Cell, 6, 893-905 (1994).
139. Moore, R. C., Durso, N. A., and Cyr, R. J., Elongation factor-1α stabilizes microtubules in a calcium/calmodulin-dependent manner. Cell Motil. Cytoskeleton, 41, 168-180 (1998).
140. Moore, R. C. and Cyr, R. J., Association between elongation factor-1a and microtubules in vivo is domain dependent and conditional. Cell Motil. Cytoskel., 45, 279-292 (2000).
141. Kaibuchi, K., Kuroda, S., and Amano, M., Regulation of the cytoskeleton and cell adhesion by the rho family GTPases in mammalian cells. Annu. Rev. Biochem., 68, 459-486 (1999).
142. Izawa, T., Fukata, Y., Kimura, T., Iwamatsu, A., Dohi, K., and Kaibuchi, K., Elongation factor-1α is a novel substrate of Rho-associated kinase. Biochem. Biophysi. Res. Comm., 278, 72-78 (2000).
143. Gonen, H., Smith, C. E., Siegel, N. R., Kahana, C., Merrick, W. C., Chakraburtty, K., Schwartz, A. L., and Ciechanover, A., Protein synthesis elongation factor EF-1a is essential for ubiquitin-dependent degradation of certain N α-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proc. Natl. Acad. Sci. USA, 91, 7648-7652 (1994).
144. Gonen, H., Dickman, D., Schwartz, A. L., and Ciechanover, A., Protein synthesis elongation factor EF-1α is an isopeptidase essential for ubiquitin-dependent degradation of certain proteolytic substrates. Adv. Exp. Med. Biol., 389, 209-219 (1996).
145. Richarme, G., Protein-disulfide isomerase activity of elongation factor EF-Tu. Biochem. Biophys. Res. Commun., 252, 156-161 (1998).
146. Atkins, J. F. and Gesteland, R. F., The twenty-first amino acid. Nature, 407, 463-465 (2000).
147. Bock, A., Biosynthesis of selenoproteins-an overview. BioFactors, 11, 77-78 (2000).
148. 75Se] SeCys-tRNA is different from EF-1α. FEBS Lett., 347, 137-142 (1994).
149. Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., and Krol, A., Characterizaiton of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J., 19, 4796-4805 (2000).
150. Tujebajeva, R. M., Copeland, P. R., Xu, X.-M., Carlson, B. A., Harney, J. W., Driscoll, D. M., Hatfield, D. L., and Berry, M. J., Decoding apparatus for eukaryotic selenocysteine insertion. EMBO Rep., 1, 158-163 (2000).
151. Copeland, P. R., Fletcher, J. E., Carlson, B. A., Hatfield, D. L., and Driscoll, D. M., A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. EMBO J., 19, 306-314 (2000).
152. Hill, K. E., Lloyd, R. S., Yang, J. G., Read, R., and Burk, R. F., The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame. J. Biol. Chem., 266, 10050-10053 (1991).
153. Gangwani, L., Mikrut, M., Galcheva-Gargova, Z., and Davis, R. J., Interaction of ZPR1 with translation elongation factor-1α in proliferating cells. J. Cell Biol., 143, 1471-1484 (1998).
154. Marchesi, V. T. and Ngo, N., In vitro assembly of multiprotein complexes containing a, b, and g tubulin, heat shock protein HSP70, and elongation factor 1α. Proc. Natl. Acad. Sci. USA, 90, 3028-3032 (1993).
155. Lund, E. and Dahlberg, J. E., Proofreading and aminoacylation of tRNAs before export from the nucleus. Science, 282, 2082-2085 (1998).
156. Kruse, C., Willkomm, D. K., Grunweller, A., Vollbrandt, T., Sommer, S., Busch, S., Pfeiffer, T., Brinkmann, J., Hartmann, R. K., and Muller, P. K., Export and transport of tRNA are coupled to a multi-protein complex. Biochem. J., 346, 107-115 (2000).
157. Kitamoto, N., Matsui, J., Kawai, Y., Kato, A., Yoshino, S., Ohmiya, K., and Tsukagoshi, N., Utilization of the TEF1-α gene (TEF1) promoter for expression of polygalacturonase genes, pgaA and pgaB, in Aspergillus oryzae. Appl. Microbiol. Biotechnol., 50, 85-92 (1998).
158. Edamatsu, H., Kaziro, Y., and Itoh, H., Inducible high-level expression vector for mammalian cells, pEF-LAC carrying human elongation factor 1a promoter and lac operator. Gene, 187, 289-294 (1997).
159. Kinoshita, M., Kani, S., Ozato, K., and Wakamatsu, Y., Activity of the medaka translation elongation factor 1α-A promoter examined using the GFP gene as a reporter. Dev. Growth Differ., 42, 469-478 (2000).
160. Gopalkrishnan, R. V., Christiansen, K. A., Goldstein, N. I., DePinho, R. A., and Fisher, P. B., Use of the human EF-1 promoter for expression can significantly increase success in establishing stable cell lines with consistent expression: a study using the tetracycline-inducible system in human cancer cells. Nucl. Acids Res., 27, 4775-4782 (1999).
161. Tokushige, K., Moradpour, D., Wakita, T., Geissler, M., Hayashi, N., and Wands, J. R., Comparison between cytomegalovirus promoter and elongation factor-1α promoter-driven constructs in the establishment of cell lines expressing hepatitis C virus core protein. J. Virol. Methods, 64, 73-80 (1997).
162. Mimori, K., Mori, M., Inoue, H., Ueo, H., Mafune, K., Akiyoshi, T., and Sugimachi, K., Elongation factor 1γ mRNA expression in oesophageal carcinoma. Gut., 38, 66-70 (1996).
163. Sun, Y., Lin, J., Katz, A. E., and Fisher, P. B., Human prostatic carcinoma oncogene PTI-1 is expressed in human tumor cell lines and prostate carcinoma patient blood samples. Cancer Res., 57, 18-23 (1997).
164. Khalyfa, A., Carlson, B. M., Carlson, J. A., and Wang, E., Toxin injury-dependent switched expression between EF-1α and its sister, S1, in rat skeletal muscle. Dev. Dyn., 216, 267-273 (1999).
165. Mendelsohn, J. and Baselga, J., The EGF receptor family as targets for cancer therapy. Oncogene, 19, 6550-6565 (2000).
166. Pegram, M. D., Lipton, A., Hayes, D. F., Weber, B. L., Baselga, J. M., Tripathy, D., Baly, D., Baughman, S. A., Twaddell, T., Glaspy, J. A., and Slamon, D. J., Phase II study of receptor-enhanced chemosensitivity using recombinant humanized anti-p185HER2/neu monoclonal antibody plus cisplatin in patients with HER2/neu-overexpressing metastatic breast cancer refractory to chemotherapy treatment. J. Clin. Oncol., 16, 2659-2671 (1998).
167. Debinski, W., Obiri, N. I., Pastan, I., and Puri, R. K., A novel chimeric protein composed of interleukin 13 and Pseudomonas exotoxin is highly cytotoxic to human carcinoma cells expressing receptors for interleukin13 and interleukin 4. J. Biol. Chem., 270, 16775-16780 (1995).
168. Davey, R. T., Boenning, C. M., Herpin, B. R., Batts, D. H., Metcalf, J. A., Wathen, L., Cox, S. R., Polis, M. A., Kovacs, J. A., and Falloon, J., Use of recombinant soluble CD4 Pseudomonas exotoxin, a novel immunotoxin, for treatment of persons infected with human immunodeficiency virus. J. Infect. Dis., 170, 1180-1188 (1994).
169. Schmidt, M., Reiser, P., Hills, D., Gullick, W. J., and Wels, W., Expression of an oncogenic mutant EGF receptor markedly increases the sensitivity of cells to an EGF-receptor-specific antibody-toxin. Int. J. Cancer, 75, 878-884 (1998).
170. Galasinski, W., Chlabicz, J., Paszkiewicz-Gadek, A., Marcinkiewicz, C., and Gindzienski, A., The substances of plant origin that inhibit protein biosynthesis. Acta. Pol. Pharm., 53, 311-318 (1996).
171. Endo, Y. and Tsurugi, K., RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem., 262, 8128-8130 (1987).
172. Habben, J. E., Moro, G. L., Hunter, B. G., Hamaker, B. R., and Larkins, B. A., Elongation factor 1a concentration is highly correlated with the lysine content of maize endosperm. Proc. Natl. Acad. Sci. USA, 92, 8640-8644 (1995).
173. Sun, Y., Carneiro, N., Clore, A. M., Moro, G. L., Habben, J. E., and Larkins, B. A., Characterization of maize elongation factor 1A and its relationship to protein quality in the endosperm. Plant Physiol., 115, 1101-1107 (1997).
174. Carneiro, N. P., Hughes, P. A., and Larkins, B. A., The eEFIA gene family is differentially expressed in maize endosperm. Plant Mol. Biol., 41, 801-813 (1999).
175. Wang, X., Woo, Y.-m., Kim, C. S., and Larkins, B. A., Quantitative trait locus mapping of loci influencing elongation factor 1α content in maize endosperm. Plant Physiol., 125, 1271-1282 (2001).
176. Kobayashi, S., Kidou, S., and Ejiri, S., Detection and characterization of glutathione S-transferase activity in rice EF-1ββ’γ and EF-1γ expressed in E. coli. Biochem. Biophys. Res. Commun., 288, 509-514 (2001).