Alternative titles; symbols
HGNC Approved Gene Symbol: EEF1G
Cytogenetic location: 11q12.3 Genomic coordinates (GRCh38): 11:62,559,596-62,573,891 (from NCBI)
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha (EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma, and EF1-delta (EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome, and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta, -gamma, and -delta subunits (Sanders et al., 1996).
Using RT-PCR with degenerate oligonucleotides based on 2 peptides conserved between Artemia and Xenopus EF1-gamma, Sanders et al. (1992) isolated a human fibroblast cDNA encoding EEF1G. The predicted 437-amino acid human protein is 60% and 85% similar to the Artemia and Xenopus proteins, respectively.
Using computer methods for protein sequence analyses, Koonin et al. (1994) found that EEF1G contains an N-terminal domain related to the theta class of glutathione S-transferases (GSTs; e.g., 600436). They proposed that the GST domain in EEF1G is involved in regulating the assembly of multisubunit complexes containing EEF1G and aminoacyl-tRNA synthetases.
By immunofluorescence analysis, Sanders et al. (1996) found that EF1-beta, -gamma, and -delta showed a perinuclear distribution and colocalized with an endoplasmic reticulum resident protein in human foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear staining and diffuse cytoplasmic staining.
Using Western blot and immunohistochemical analyses, Cao et al. (2014) showed that EEF1B-alpha, -delta, and -gamma were widely expressed in human and mouse cell lines and tissues and at different stages of mouse development. Immunofluorescence analysis on sections of mouse spinal cord revealed that all 3 Eef1b subunits colocalized with Eef1a2 (602959) in neurons, and EEF1B-EEF1A2 colocalization was confirmed in HeLa cells.
Gross (2022) mapped the EEF1G gene to chromosome 11q12.3 based on an alignment of the EEF1G sequence (GenBank BC000384) with the genomic sequence (GRCh38).
Using Northern blot analysis, Sanders et al. (1992) found that expression of the Eef1g, Eef1b2, and Ef1a genes was 20-fold higher in cultured rat cells than in rat tissues. However, oncogenic transformation of human and rat cells did not have a major effect on EF1 mRNA levels. Sanders et al. (1992) suggested that the levels of the EF1 mRNAs rise as a result of a loss of contact inhibition, leading to the increases seen in tumors and cultured cells.
Lew et al. (1992) found that EEF1G mRNA was expressed at higher levels in 7 of 9 pancreatic tumors than in the corresponding normal tissues.
Cao et al. (2014) showed that knockdown of each EEF1B subunit in human cell lines reduced cell viability, decreased the proportion of cells in S and G2/M phases, and increased the proportion of cells in G0/G1 phase.
Cao, Y., Portela, M., Janikiewicz, J., Doig, J., Abbott, C. M. Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2. PLoS One 9: e114117, 2014. [PubMed: 25436608] [Full Text: https://doi.org/10.1371/journal.pone.0114117]
Gross, M. B. Personal Communication. Baltimore, Md. 1/14/2022.
Koonin, E. V., Mushegian, A. R., Tatusov, R. L., Altschul, S. F., Bryant, S. H., Bork, P., Valencia, A. Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling. Protein Sci. 3: 2045-2054, 1994. [PubMed: 7703850] [Full Text: https://doi.org/10.1002/pro.5560031117]
Lew, Y., Jones, D. V., Mars, W. M., Evans, D., Byrd, D., Frazier, M. L. Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer. Pancreas 7: 144-152, 1992. [PubMed: 1372736] [Full Text: https://doi.org/10.1097/00006676-199203000-00003]
Sanders, J., Brandsma, M., Janssen, G. M. C., Dijk, J., Moller, W. Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1-beta-gamma-delta in the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996. [PubMed: 8743958] [Full Text: https://doi.org/10.1242/jcs.109.5.1113]
Sanders, J., Maassen, J. A., Moller, W. Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation. Nucleic Acids Res. 20: 5907-5910, 1992. [PubMed: 1461723] [Full Text: https://doi.org/10.1093/nar/20.22.5907]