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Gene Review

EEF1A1  -  eukaryotic translation elongation factor 1...

Bos taurus

Synonyms: EF-1-alpha-1, EF-Tu, eEF1A-1
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Disease relevance of EEF1A1

  • We report herewith that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins as do molecular chaperones that are involved in protein folding and protein renaturation after stress [1].
  • The conserved association of eEF1A with virus molecules involved in genome replication and the postulated role of pestivirus and hepacivirus NS5A in replication indicate that this interaction may play a role in the replication of BVDV [2].
  • In this study, we identified and characterised the ef-1alpha locus of Babesia bovis, a causative agent of bovine babesiosis, and examined the transcriptional activity of the EF-1alpha promoter [3].
  • Genetic and antigenic characterisation of elongation factor Tu from Mycoplasma mycoides subsp. mycoides SC [4].
  • The EF-Ts bound to two eubacterial EF-Tu species (E.coli and Thermus thermophilus) [5].

High impact information on EEF1A1

  • Homologies are found between the sequence of the alpha subunit and those of other guanine nucleotide-binding proteins, the ras proteins, peptide chain elongation factors EF-Tu and EF-G, and the initiation factor IF2 [6].
  • N-Ethylmaleimide inhibits the activity of EF-Tu.Tsmt in polymerization and in ribosome binding [7].
  • GDP and the non-hydrolyzable GTP analog guanyl-5'-yl imidodiphosphate are also capable of facilitating ternary complex formation with EF-Tu.Tsmt, but are less effective [7].
  • In contrast to the bacterial EF-Tu and the EF-Tu from the chloroplast of E. gracilis, the ability of the mitochondrial factor to catalyze polymerization is not inhibited by the antibiotic kirromycin [8].
  • Neither of these GTP gamma S-sensitive cysteines are in those regions of alpha 39 which are highly homologous to the GTP-binding site of elongation factor Tu (Jurnak, F. (1985) Science 230, 32-36) [9].

Chemical compound and disease context of EEF1A1


Biological context of EEF1A1


Anatomical context of EEF1A1

  • Remarkably, in vitro renaturation occurs at the molar ratio of eEF1A to ARS equivalent to that found in the cytoplasm of higher eukaryotic cells [15].
  • Recombinant nematode EF-Ts purified from Escherichia coli bound both of these molecules and also stimulated the translational activity of EF-Tu, indicating that the nematode EF-Ts homolog is a functional EF-Ts protein of mitochondria [5].

Associations of EEF1A1 with chemical compounds


Regulatory relationships of EEF1A1


Other interactions of EEF1A1

  • The full recovery of the phenylalanyl- (PheRS) and seryl-tRNA synthetase (SerRS) activities was achieved in the presence of 4 microM eEF1A, while bovine serum albumin at similar concentration had no renaturation effect [15].
  • The relative molecular mass of the purified factors have been determined as: EF-1 alpha, 50,000; EF-1 beta, 30,000; the EF-1 gamma-like component, 49,000; EF-2, 85,000 [19].

Analytical, diagnostic and therapeutic context of EEF1A1


  1. Chaperone properties of bacterial elongation factor EF-Tu. Caldas, T.D., El Yaagoubi, A., Richarme, G. J. Biol. Chem. (1998) [Pubmed]
  2. The NS5A protein of bovine viral diarrhoea virus interacts with the alpha subunit of translation elongation factor-1. Johnson, C.M., Perez, D.R., French, R., Merrick, W.C., Donis, R.O. J. Gen. Virol. (2001) [Pubmed]
  3. Characterization and gene expression of Babesia bovis elongation factor-1alpha. Suarez, C.E., Norimine, J., Lacy, P., McElwain, T.F. Int. J. Parasitol. (2006) [Pubmed]
  4. Genetic and antigenic characterisation of elongation factor Tu from Mycoplasma mycoides subsp. mycoides SC. Alonso, J.M., Prieto, M., Parra, F. Vet. Microbiol. (2002) [Pubmed]
  5. Characterization of the interaction between the nucleotide exchange factor EF-Ts from nematode mitochondria and elongation factor Tu. Ohtsuki, T., Sakurai, M., Sato, A., Watanabe, K. Nucleic Acids Res. (2002) [Pubmed]
  6. GTPase of bovine rod outer segments: the amino acid sequence of the alpha subunit as derived from the cDNA sequence. Yatsunami, K., Khorana, H.G. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  7. Interaction of animal mitochondrial EF-Tu.EF-Ts with aminoacyl-tRNA, guanine nucleotides, and ribosomes. Schwartzbach, C.J., Spremulli, L.L. J. Biol. Chem. (1991) [Pubmed]
  8. Bovine mitochondrial protein synthesis elongation factors. Identification and initial characterization of an elongation factor Tu-elongation factor Ts complex. Schwartzbach, C.J., Spremulli, L.L. J. Biol. Chem. (1989) [Pubmed]
  9. Reactive sulfhydryl groups of alpha 39, a guanine nucleotide-binding protein from brain. Location and function. Winslow, J.W., Bradley, J.D., Smith, J.A., Neer, E.J. J. Biol. Chem. (1987) [Pubmed]
  10. Mutagenesis of glutamine 290 in Escherichia coli and mitochondrial elongation factor Tu affects interactions with mitochondrial aminoacyl-tRNAs and GTPase activity. Hunter, S.E., Spremulli, L.L. Biochemistry (2004) [Pubmed]
  11. Rapid communication: nucleotide sequence of the bovine elongation factor 1 alpha cDNA1. Kojima, T., Oshima, K., Watanabe, H., Komatsu, M. J. Anim. Sci. (2002) [Pubmed]
  12. Identification of novel antigenic proteins in a complex Anaplasma marginale outer membrane immunogen by mass spectrometry and genomic mapping. Lopez, J.E., Siems, W.F., Palmer, G.H., Brayton, K.A., McGuire, T.C., Norimine, J., Brown, W.C. Infect. Immun. (2005) [Pubmed]
  13. The postsynaptic density: constituent and associated proteins characterized by electrophoresis, immunoblotting, and peptide sequencing. Walsh, M.J., Kuruc, N. J. Neurochem. (1992) [Pubmed]
  14. Primary structure of the alpha-subunit of bovine adenylate cyclase-stimulating G-protein deduced from the cDNA sequence. Nukada, T., Tanabe, T., Takahashi, H., Noda, M., Hirose, T., Inayama, S., Numa, S. FEBS Lett. (1986) [Pubmed]
  15. Chaperone-like activity of mammalian elongation factor eEF1A: renaturation of aminoacyl-tRNA synthetases. Lukash, T.O., Turkivska, H.V., Negrutskii, B.S., El'skaya, A.V. Int. J. Biochem. Cell Biol. (2004) [Pubmed]
  16. A factor protecting mammalian [75Se]SeCys-tRNA is different from EF-1 alpha. Yamada, K., Mizutani, T., Ejiri, S., Totsuka, T. FEBS Lett. (1994) [Pubmed]
  17. Transfer ribonucleic acid populations in concanavalin-A-stimulated bovine lymphocytes. Derwenskus, K.H., Sprinzl, M. Biochim. Biophys. Acta (1986) [Pubmed]
  18. Characterization of the elongation factors from calf brain. 2. Functional properties of EF-1 alpha, the action of physiological ligands and kirromycin. Crechet, J.B., Parmeggiani, A. Eur. J. Biochem. (1986) [Pubmed]
  19. Characterization of the elongation factors from calf brain. 1. Purification, molecular and immunological properties. Crechet, J.B., Canceill, D., Bocchini, V., Parmeggiani, A. Eur. J. Biochem. (1986) [Pubmed]
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