Elongation factor-1 is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. EF-1 is a major protein of eukaryotic cells and exists as a heterotrimer consisting of the subunits EF1-alpha , EF1-beta, and EF1-gamma. There is also an EF1-delta, a form homologous to EF1-beta. Hence, 2 species of EF-1 with composition EF1-alpha/beta/gamma or EF1-alpha/delta/gamma can be formed (van Damme et al., 1990) EF-1 comprises 2 distinct functional domains: a nucleotide binding domain provided by EF1-alpha and a nucleotide exchange protein complex EF1-beta/gamma.
Guo et al. (1997) reported the presence of constitutive expression of elongation factor 1alpha (EF-1 alpha) mRNA in murine ovaries and granulosa cells treated with PMSG.
von der Kammer et al. (1991) identified a cDNA clone lambda HGP34, containing an EcoRI insert of 829 bp from a cDNA library in lambda gt11 derived from poly (A+)RNA of human ovarian granulosa cells. The derived amino acid sequence, corresponding to a protein of 225 amino acids, shows a high degree of homology to elongation factor 1 beta (EF-1 beta) of Artemia salina (57%) and known peptide sequences of Xenopus laevis EF-1 beta (86%). The protein coded for by pHGP34 represents human EF-1 beta. Northern analysis reveals an EF-1 beta specific mRNA of 900 bp.
Abdallah et al. (1991)reported germ cell-specific expression of a gene
encoding eukaryotic translation elongation factor 1 alpha (eEF-1 alpha) and
generation of eEF-1 alpha retropseudogenes in Xenopus laevis.