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

• Mutagenesis of glutamine 290 in Escherichia coli and mitochondrial elongation factor Tu affects interactions with mitochondrial aminoacyl-tRNAs and GTPase activity [10].
• The full recombinant EF-Tu was produced in E. coli, after correction of an unusual tryptophan codon by site-directed mutagenesis, and used to investigate anti-EF-Tu circulating antibodies in bovine sera [4].

Biological context of EEF1A1

• Rapid communication: nucleotide sequence of the bovine elongation factor 1 alpha cDNA1 [11].
• Among the 21 newly described antigenic proteins, 14 are annotated in the A. marginale genome and include type IV secretion system proteins, elongation factor Tu, and members of the MSP2 superfamily [12].
• The PSD fraction is enriched for spectrin, actin, tublin and microtubule associated protein II, myosin, enzymes of glycolysis, creatine kinase, elongation factor 1 alpha, and receptor protein [13].
• Comparison of the amino acid sequences of the alpha-subunits of Gs and transducin reveals that some of the highly conserved regions show sequence homology with elongation factor-Tu and ras p21 proteins and correspond to functional regions of guanine nucleotide-binding proteins [14].
• Because of its high level of transcription, the EF-1alpha promoter has been utilised to drive exogenous gene expression in transfected cells [3].

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

• A factor protecting mammalian [75Se]SeCys-tRNA is different from EF-1 alpha [16].
• Upon monitoring the tRNA isoacceptor distribution by affinity chromatography on immobilized elongation factor Tu and subsequent two-dimensional gel electrophoresis, a preferential synthesis of particular lysine- and threonine-accepting tRNAs was observed upon mitogenic stimulation [17].

Regulatory relationships of EEF1A1

• EF-1 beta strongly enhances the dissociation rate of the EF-1 alpha X GDP complex and to a lesser extent of the EF-1 alpha X GTP complex [18].

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

• In addition to performing these two chromatographies, we investigated pure EF-1 alpha from Bombyx mori but could not detect any SePF activity in B. mori EF-1 alpha [16].

References