The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

EEF1A1  -  eukaryotic translation elongation factor 1...

Homo sapiens

Synonyms: CCS-3, CCS3, EE1A1, EEF-1, EEF1A, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of EEF1A1

  • To generate specific tools for, in particular, localization studies of the eukaryotic elongation factor 1A (eEF1A), we have applied phage display in various formats to affinity-improve and map epitopes of two previously isolated, low-affinity single-chain Fv (scFv) G3 and D1 [1].
  • In contrast, PTI-1 RNA is not detected in human melanoma, neuroblastoma, osteosarcoma, normal cerebellum, or glioblastoma multiforme cell lines [2].
  • By using a pair of primers recognizing a 280-bp region within the 630-bp 5' PTI-1 sequence, reverse transcription-PCR detects PTI-1 expression in patient-derived prostate carcinomas but not in normal prostate or benign hypertrophic prostate tissue [2].
  • A putative dominant-acting nude mouse prostatic carcinoma tumor-inducing gene, PTI-1, has been cloned that is expressed in patient-derived human prostatic carcinomas but not in benign prostatic hypertrophy or normal prostate tissue [2].
  • The EFG1-mutant patient had early-onset Leigh syndrome, whereas the EFTu-mutant patient had severe infantile macrocystic leukodystrophy with micropolygyria [3].

High impact information on EEF1A1


Chemical compound and disease context of EEF1A1


Biological context of EEF1A1

  • The aptameric oligonucleotides GT were found to exert a selective, specific and dose-dependent cell growth inhibition effect on a variety of human cancer cells by recognising specific nuclear proteins and among these in particular an isoform of the eukaryotic elongation factor 1A1 (EEF1A1) [13].
  • Screening a human prostatic carcinoma (LNCaP) cDNA library with a 214-bp DNA fragment found by DD permitted the cloning of a full-length 2.0-kb PTI-1 cDNA [2].
  • Sequence analysis indicates that PTI-1 is a gene containing a 630-bp 5' sequence and a 3' sequence homologous to a truncated and mutated form of human elongation factor 1 alpha [2].
  • These results indicate that PTI-1 may be a member of a class of oncogenes that could affect protein translation and contribute to carcinoma development in human prostate and other tissues [2].
  • Fluorescence resonance energy transfer was used to observe aminoacyl-tRNA (aa-tRNA) stably accommodating into the aminoacyl site (A site) of the ribosome via a multistep, elongation factor-Tu dependent process [14].

Anatomical context of EEF1A1

  • In eukaryotic cells the concentration of EF-1 alpha exceeds that of the complex beta gamma delta by a factor of 5-10 [15].
  • Apparently, the common characteristic of these GTPases is an extensive consensus structural unit that possibly accounts for a similar interaction with the ribosome and is composed of two domains homologous to the G domain and domain II in EF-Tu and EF-G [16].
  • Over-expression of either EFTu or EFTs in control and patient fibroblasts produced dominant negative effects, indicating that the relative abundance of these factors is an important determinant of translation efficiency [17].
  • We discuss the possible role of EF-Tumt chaperone activity in protein quality control in mitochondria, with regard to the recently reported in vivo chaperone function of eEF1A [18].
  • Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha [19].

Associations of EEF1A1 with chemical compounds

  • Subsequent analysis identified the translation elongation factor, eEF1A, and its guanine nucleotide exchange factor, eEF1Bbeta, as TCTP-interacting partners [20].
  • This novel posttranslational modification may represent an important alteration of EF-1 alpha, comparable to the regulatory effects of posttranslational methylation of EF-1 alpha lysine residues [21].
  • EF-1 beta gamma decreases the amount of EF-1 alpha required for polyphenylalanine synthesis about 20-fold [22].
  • Although entry of the charged transfer messenger RNA (tmRNA) into the ribosome proceeded in the absence of elongation factor (EF-Tu) and in the presence of EF-Tu and the antibiotic kirromycin, evidence was found for the involvement of EF-Tu in trans-translation initiation [23].
  • Metabolic radiolabeling with [3H] ethanolamine shows that, in all cells examined, EF-1 alpha is the major radiolabeled protein [21].

Physical interactions of EEF1A1


Regulatory relationships of EEF1A1

  • EF-1 beta gamma enhances the ability to EF-1 alpha to support the binding of Phe-tRNA to the ribosomes and enhances the GTPase activity of EF-1 alpha [22].
  • Association of the 5'HS4 sequence of the chicken beta-globin locus control region with human EF1 alpha gene promoter induces ubiquitous and high expression of human CD55 and CD59 cDNAs in transgenic rabbits [26].
  • To evaluate enzyme replacement therapy for GSD II patients, we have expressed human GAA cDNA in Chinese hamster ovary-K1 cells utilising a vector that places the cDNA under the transcriptional control of the human polypeptide chain elongation factor 1 alpha gene promoter [27].

Other interactions of EEF1A1

  • Additionally, MS analysis also identified eEF1A as a TCTP interactor [20].
  • Two differentially expressed isoforms of eEF1A, designated eEF1A-1 and eEF1A-2, are found in mammals [28].
  • Two candidate genes, EEF1A1 and IMPG1, were selected from the region between D6S280 and D6S1644 markers where the families are linked [29].
  • It can also export the RNA binding proteins ILF3 and elongation factor EF1A [30].
  • Southern analysis indicates that EF-1 beta in the human genome, like EF-1 alpha, appears to be specified by more than one gene [31].

Analytical, diagnostic and therapeutic context of EEF1A1


  1. Generation and epitope mapping of high-affinity scFv to eukaryotic elongation factor 1A by dual application of phage display. Kjaer, S., Wind, T., Ravn, P., Østergaard, M., Clark, B.F., Nissim, A. Eur. J. Biochem. (2001) [Pubmed]
  2. Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display. Shen, R., Su, Z.Z., Olsson, C.A., Fisher, P.B. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  3. Infantile Encephalopathy and Defective Mitochondrial DNA Translation in Patients with Mutations of Mitochondrial Elongation Factors EFG1 and EFTu. Valente, L., Tiranti, V., Marsano, R.M., Malfatti, E., Fernandez-Vizarra, E., Donnini, C., Mereghetti, P., De Gioia, L., Burlina, A., Castellan, C., Comi, G.P., Savasta, S., Ferrero, I., Zeviani, M. Am. J. Hum. Genet. (2007) [Pubmed]
  4. The transorientation hypothesis for codon recognition during protein synthesis. Simonson, A.B., Lake, J.A. Nature (2002) [Pubmed]
  5. pH, EF-1alpha and the cytoskeleton. Liu, G., Edmonds, B.T., Condeelis, J. Trends Cell Biol. (1996) [Pubmed]
  6. Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. Calado, A., Treichel, N., Müller, E.C., Otto, A., Kutay, U. EMBO J. (2002) [Pubmed]
  7. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. Bohnsack, M.T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E., Görlich, D. EMBO J. (2002) [Pubmed]
  8. Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein. Cimarelli, A., Luban, J. J. Virol. (1999) [Pubmed]
  9. The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Brands, J.H., Maassen, J.A., van Hemert, F.J., Amons, R., Möller, W. Eur. J. Biochem. (1986) [Pubmed]
  10. Crosslinking of tRNA containing a long extra arm to elongation factor Tu by trans-diamminedichloroplatinum(II). Rasmussen, N.J., Wikman, F.P., Clark, B.F. Nucleic Acids Res. (1990) [Pubmed]
  11. Overexpression of ribosomal proteins L4 and L5 and the putative alternative elongation factor PTI-1 in the doxorubicin resistant human colon cancer cell line LoVoDxR. Bertram, J., Palfner, K., Hiddemann, W., Kneba, M. Eur. J. Cancer (1998) [Pubmed]
  12. Translational arrest in hypoxic potato tubers is correlated with the aberrant association of elongation factor EF-1 alpha with polysomes. Vayda, M.E., Shewmaker, C.K., Morelli, J.K. Plant Mol. Biol. (1995) [Pubmed]
  13. Aptameric GT oligomers need to be complexed to ethoxylated polyethylenimine as pre-paired duplexes to efficiently exert their cytotoxic activity in human lymphoblastic cancer cells. Scaggiante, B., Dapas, B., Perissin, L., Manzini, G. Biochimie (2005) [Pubmed]
  14. tRNA dynamics on the ribosome during translation. Blanchard, S.C., Kim, H.D., Gonzalez, R.L., Puglisi, J.D., Chu, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  15. Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. Sanders, J., Brandsma, M., Janssen, G.M., Dijk, J., Möller, W. J. Cell. Sci. (1996) [Pubmed]
  16. Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation. Avarsson, A. J. Mol. Evol. (1995) [Pubmed]
  17. The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1. Antonicka, H., Sasarman, F., Kennaway, N.G., Shoubridge, E.A. Hum. Mol. Genet. (2006) [Pubmed]
  18. Chaperone properties of Mammalian mitochondrial translation elongation factor tu. Suzuki, H., Ueda, T., Taguchi, H., Takeuchi, N. J. Biol. Chem. (2007) [Pubmed]
  19. Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha. Ann, D.K., Wu, M.M., Huang, T., Carlson, D.M., Wu, R. J. Biol. Chem. (1988) [Pubmed]
  20. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Cans, C., Passer, B.J., Shalak, V., Nancy-Portebois, V., Crible, V., Amzallag, N., Allanic, D., Tufino, R., Argentini, M., Moras, D., Fiucci, G., Goud, B., Mirande, M., Amson, R., Telerman, A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  21. Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. Whiteheart, S.W., Shenbagamurthi, P., Chen, L., Cotter, R.J., Hart, G.W. J. Biol. Chem. (1989) [Pubmed]
  22. Purification and characterization of three elongation factors, EF-1 alpha, EF-1 beta gamma, and EF-2, from wheat germ. Lauer, S.J., Burks, E., Irvin, J.D., Ravel, J.M. J. Biol. Chem. (1984) [Pubmed]
  23. SmpB triggers GTP hydrolysis of elongation factor Tu on ribosomes by compensating for the lack of codon-anticodon interaction during trans-translation initiation. Shimizu, Y., Ueda, T. J. Biol. Chem. (2006) [Pubmed]
  24. Identification of the sites in the eukaryotic elongation factor 1 alpha involved in the binding of elongation factor 1 beta and aminoacyl-tRNA. van Damme, H.T., Amons, R., Möller, W. Eur. J. Biochem. (1992) [Pubmed]
  25. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi, S., Aevarsson, A., Garber, M., Zheltonosova, J., Liljas, A. Structure (1996) [Pubmed]
  26. Association of the 5'HS4 sequence of the chicken beta-globin locus control region with human EF1 alpha gene promoter induces ubiquitous and high expression of human CD55 and CD59 cDNAs in transgenic rabbits. Taboit-Dameron, F., Malassagne, B., Viglietta, C., Puissant, C., Leroux-Coyau, M., Chéreau, C., Attal, J., Weill, B., Houdebine, L.M. Transgenic Res. (1999) [Pubmed]
  27. Isolation and characterisation of a recombinant, precursor form of lysosomal acid alpha-glucosidase. Fuller, M., Van der Ploeg, A., Reuser, A.J., Anson, D.S., Hopwood, J.J. Eur. J. Biochem. (1995) [Pubmed]
  28. The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity. Bischoff, C., Kahns, S., Lund, A., Jørgensen, H.F., Praestegaard, M., Clark, B.F., Leffers, H. Genomics (2000) [Pubmed]
  29. Molecular genetic analysis of two functional candidate genes in the autosomal recessive retinitis pigmentosa, RP25, locus. Abd El-Aziz, M.M., El-Ashry, M.F., Barragan, I., Marcos, I., Borrego, S., Antiñolo, G., Bhattacharya, S.S. Curr. Eye Res. (2005) [Pubmed]
  30. Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5. Chen, T., Brownawell, A.M., Macara, I.G. Mol. Cell. Biol. (2004) [Pubmed]
  31. Human elongation factor 1 beta: cDNA and derived amino acid sequence. von der Kammer, H., Klaudiny, J., Zimmer, M., Scheit, K.H. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  32. Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family. Madsen, H.O., Poulsen, K., Dahl, O., Clark, B.F., Hjorth, J.P. Nucleic Acids Res. (1990) [Pubmed]
  33. Elongation factor Tu localized on the exterior surface of the small ribosomal subunit. Langer, J.A., Lake, J.A. J. Mol. Biol. (1986) [Pubmed]
  34. Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3. Lund, A., Knudsen, S.M., Vissing, H., Clark, B., Tommerup, N. Genomics (1996) [Pubmed]
WikiGenes - Universities