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Gene Review

Eef1a2  -  eukaryotic translation elongation factor 1...

Mus musculus

Synonyms: EF-1-alpha-2, Eef1a, Eef1al, Elongation factor 1-alpha 2, Eukaryotic elongation factor 1 A-2, ...
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Disease relevance of Eef1a2


High impact information on Eef1a2

  • Expression of Eef1a2 takes over from Eef1a in heart and muscle at precisely the time at which the wasted phenotype becomes manifest [6].
  • In addition, studies of COS cells transfected with the S1 gene containing small changes around the first AUG suggest that bicistronic mRNA translation is regulated at the level of elongation [7].
  • To determine if uninfected cells can utilize bicistronic genes, a bovine papilloma virus-based vector system was used to select mouse C127 cell lines containing multiple integrated copies of the reovirus S1 gene [7].
  • Enzyme activity in wst/wst mice is reduced to 38% of that found in the erythrocytes from control mice, and the apparent Km for adenosine is reduced to 51% of control [8].
  • The 5' end of the gene has been defined, both by nuclease S1 protection and primer extension studies and by a functional assay in which an HPRT minigene, capable of expression in cultured cells, was created by ligating the 5' end of the gene onto wild-type human HPRT cDNA [9].

Biological context of Eef1a2

  • Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress [10].
  • Thus, our results suggest that eEF1A-2 interacts with Prdx-I to functionally provide cells with extraordinary resistance to oxidative stress-induced cell death [10].
  • Adenosine deaminase, Ada, is in mouse chromosome 2H3, and is not allelic with wasted, wst [11].
  • Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis [12].
  • After activation with concanavalin A, however, splenocytes from wst/wst mice showed a lower percentage of cells in S phase compared with that in controls [1].

Anatomical context of Eef1a2

  • In adult mammalian tissues, isoform eEF1A-1 is present in all tissues except neurons, cardiomyocytes, and myotubes, where its isoform, eEF1A-2, is the only form expressed [10].
  • Here we show that Prdx-I coimmunoprecipitates with eEF1A-2 from extracts of both cultured cells and mouse tissues expressing this protein, but it does not do so with its isoform, eEF1A-1, even though the latter is abundantly present [10].
  • Peptide elongation factor eEF1A-2/S1, which shares 92% homology with eEF1A-1/EF-1alpha, is exclusively expressed in brain, heart, and skeletal muscle [12].
  • Comparison of two-dimensional gel electrophoresis patterns of proteins from wst/wst and control mouse thymus revealed that an acidic protein with a molecular mass of approximately 30 kDa was consistently expressed at lower levels in wasted mice than in controls [1].
  • We report here the isolation of a full-length cDNA from a mouse brain library and a partial-length cDNA from a human hippocampus library which share extensive sequence similarity to rat S1 cDNA [13].

Associations of Eef1a2 with chemical compounds

  • Quantitative solution hybridization demonstrated a dramatic reduction (approximately 68%) in the S1 mRNA following isoproterenol injection in proliferation-responsive parotid glands and a mild reduction (approximately 20%) of S1 steady-state messages in the proliferation-refractile submandibular glands [14].
  • Moreover, wst/wst thymocytes are more sensitive to apoptosis induced by gamma radiation, heat shock, alpha-CD3 stimulation, and dexamethasone treatment in vitro [15].
  • It is possible to fragment the DNA under appropriate conditions by the single-strand-specific nuclease S1 at the site of these A+T-rich zones and to obtain, on alkaline sucrose gradients, a bimodal pattern of DNA fragments of the size corresponding to the pattern observed by electron microscopy [16].
  • Here, we report that eEF1A2 directly binds to and activates phosphatidylinositol 4-kinase III beta (PI4KIIIbeta), an enzyme that converts phosphatidylinositol to phosphatidylinositol 4-phosphate [17].
  • A morphometric analysis of motor neurons in the spinal cord was performed on 2-hydroxyethyl methacrylate-embedded tissue from ten wst/wst mice, ten littermates (wst/+, +/+) without clinical deficits, and ten parental (+/+) control mice [18].

Regulatory relationships of Eef1a2


Other interactions of Eef1a2

  • We have focused on the protein with the highest frequency of hits, peroxiredoxin I (Prdx-I), for in-depth study of its functional implication for eEF1A-2 [10].
  • Mice that are homozygous for the recessive mutation wasted (wst) appear normal until soon after weaning, but then develop tremors and ataxia, undergo atrophy of the thymus and spleen, and die by around 28 days of age [19].
  • Lymphoproliferative responsiveness to Con A was markedly altered in the wst/wst thymus and spleen, in an age-dependent fashion, compared with normal littermates [4].
  • Northern analysis and RNase protection assays have revealed that S1 mRNA is present only in brain, heart, and muscle, while EF-1 alpha mRNA has been detected in all tissues surveyed so far [20].
  • Homozygous wabbler-lethal (wl) and wasted (wst) showed hyposensitivity which for the latter may be connected with enhanced cell killing [21].

Analytical, diagnostic and therapeutic context of Eef1a2


  1. Regulation of thymus PCNA expression is altered in radiation-sensitive wasted mice. Woloschak, G.E., Paunesku, T., Libertin, C.R., Chang-Liu, C.M., Churchill, M., Panozzo, J., Grdina, D., Gemmell, M.A., Giometti, C. Carcinogenesis (1996) [Pubmed]
  2. Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation. Roth, W.W., Bragg, P.W., Corrias, M.V., Reddy, N.S., Dholakia, J.N., Wahba, A.J. Mol. Cell. Biol. (1987) [Pubmed]
  3. Effect of DNA-damaging agents on isolated spleen cells and lung fibroblasts from the mouse mutant "wasted," a putative animal model for ataxia-telangiectasia. Inoue, T., Aikawa, K., Tezuka, H., Kada, T., Shultz, L.D. Cancer Res. (1986) [Pubmed]
  4. Longitudinal assessment of immunologic abnormalities of mice with the autosomal recessive mutation, "wasted". Goldowitz, D., Shipman, P.M., Porter, J.F., Schmidt, R.R. J. Immunol. (1985) [Pubmed]
  5. Progressive loss of motor neuron function in wasted mice: effects of a spontaneous null mutation in the gene for the eEF1 A2 translation factor. Newbery, H.J., Gillingwater, T.H., Dharmasaroja, P., Peters, J., Wharton, S.B., Thomson, D., Ribchester, R.R., Abbott, C.M. J. Neuropathol. Exp. Neurol. (2005) [Pubmed]
  6. The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1alpha, encoded by the Eef1a2 gene. Chambers, D.M., Peters, J., Abbott, C.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. Translation of bicistronic viral mRNA in transfected cells: regulation at the level of elongation. Fajardo, J.E., Shatkin, A.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  8. Deficiency of adenosine deaminase in the wasted mouse. Abbott, C.M., Skidmore, C.J., Searle, A.G., Peters, J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  9. Structure, expression, and mutation of the hypoxanthine phosphoribosyltransferase gene. Melton, D.W., Konecki, D.S., Brennand, J., Caskey, C.T. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  10. Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress. Chang, R., Wang, E. J. Cell. Biochem. (2007) [Pubmed]
  11. Adenosine deaminase, Ada, is in mouse chromosome 2H3, and is not allelic with wasted, wst. Abbott, C.M., Evans, E.P., Burtenshaw, M., Ball, S.T., Skidmore, C.J., Jones, J., Peters, J. Biochem. Genet. (1991) [Pubmed]
  12. Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. Ruest, L.B., Marcotte, R., Wang, E. J. Biol. Chem. (2002) [Pubmed]
  13. Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway. Lee, S., Ann, D.K., Wang, E. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  14. Characterization of the statin-like S1 and rat elongation factor 1 alpha as two distinctly expressed messages in rat. Ann, D.K., Lin, H.H., Lee, S., Tu, Z.J., Wang, E. J. Biol. Chem. (1992) [Pubmed]
  15. The wst gene regulates multiple forms of thymocyte apoptosis. Potter, M., Bernstein, A., Lee, J.M. Cell. Immunol. (1998) [Pubmed]
  16. Systematic punctuation of eukaryotic DNA by A+T-rich sequences. Moreau, J., Matyash-Smirniaguina, L., Scherrer, K. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  17. Binding of Elongation Factor eEF1A2 to Phosphatidylinositol 4-Kinase beta Stimulates Lipid Kinase Activity and Phosphatidylinositol 4-Phosphate Generation. Jeganathan, S., Lee, J.M. J. Biol. Chem. (2007) [Pubmed]
  18. Ultrastructural, morphometric, and immunocytochemical study of anterior horn cells in mice with "wasted" mutation. Lutsep, H.L., Rodriguez, M. J. Neuropathol. Exp. Neurol. (1989) [Pubmed]
  19. Linkage mapping around the ragged (Ra) and wasted (wst) loci on distal mouse chromosome 2. Abbott, C., Malas, S., Pilz, A., Pate, L., Ali, R., Peters, J. Genomics (1994) [Pubmed]
  20. Tissue-specific expression in mammalian brain, heart, and muscle of S1, a member of the elongation factor-1 alpha gene family. Lee, S., Francoeur, A.M., Liu, S., Wang, E. J. Biol. Chem. (1992) [Pubmed]
  21. A search for radiosensitive mouse mutants by use of the micronucleus technique. van Buul, P.P., Tuinenburg-Bolraap, A., Searle, A.G., Natarajan, A.T. Mutat. Res. (1987) [Pubmed]
  22. Isolation and characterization of the rat chromosomal gene for a polypeptide (pS1) antigenically related to statin. Ann, D.K., Moutsatsos, I.K., Nakamura, T., Lin, H.H., Mao, P.L., Lee, M.J., Chin, S., Liem, R.K., Wang, E. J. Biol. Chem. (1991) [Pubmed]
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