Disease relevance of EFB1

• The structure of the 61 kDa complex was determined with the multiple anomalous dispersion technique using three selenomethionine residues in a 11 kDa eEF1B alpha fragment generated by limited proteolysis of full-length eEF1B alpha expressed in Escherichia coli [1].

High impact information on EFB1

• The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A resolution [2].
• EF-1 is composed of a nucleotide-binding protein EF-1 alpha, and a nucleotide exchange protein complex, EF-1 beta gamma, while EF-2 catalyses the translocation of peptidyl-tRNA on the ribosome [3].
• Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Balpha are consistent with in vivo data [4].
• Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity [5].
• In this work, we demonstrate that the highly conserved C-terminal region of Saccharomyces cerevisiae EF-1beta is sufficient for normal cell growth [5].

Biological context of EFB1

• Complementation of Saccharomyces cerevisiae mutations in genes involved in translation and protein folding (EFB1 and SSB1) with Candida albicans cloned genes [6].
• We have demonstrated that the expression of Candida albicans genes involved in translation and protein folding (EFB1 and SSB1) complements the phenotype of Saccharomyces cerevisiae mutants [6].
• Exon sequences are highly homologous (74%) to S. cerevisiae EFB1, whereas intron sequence is less conserved (34% identity), and the predicted amino acid sequence shares about 73% identity [7].
• These phenotypes indicate that translation and cell growth are highly sensitive to changes in EF-1alpha and EF-1beta activity [8].
• Based on the sequence and functional homology, mutagenesis of two C-terminal residues identical in all EF-1beta protein sequences was performed, resulting in mutants with growth defects and sensitivity to translation inhibitors [5].

Associations of EFB1 with chemical compounds

• The cDNA encoded a protein of 206 amino acids which was highly homologous (about 70% homology) with Artemia salina and human EF-1 beta [9].
• Crystals of the Saccharomyces cerevisiae elongation factor eEF1A (formerly EF-1 alpha) in complex with a catalytic C-terminal fragment of the nucleotide-exchange factor eEF1B alpha (formerly EF-1 beta) were grown by the sitting-drop vapour-diffusion technique, using polyethylene glycol 2000 monomethyl ether as precipitant [1].
• However, replacement of Thr91, the sole consensus CDK phosphorylation site in pea eEF1Bbeta, with alanine allowed the pea protein to substitute for eEF1Balpha function in vivo [10].
• Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha [11].
• cDNA cloning and immunologic characterization of a novel EF-1beta allergen from Penicillium citrinum [12].

Regulatory relationships of EFB1

• The lethality of a null allele of the TEF5 gene encoding EF-1beta in Saccharomyces cerevisiae was suppressed by extra copies of the TEF2 gene encoding EF-1alpha [8].

Other interactions of EFB1

• The stimulatory effect of EF-3 is, in many respects, distinct from that of EF-1 beta [13].
• Cells lacking the catalytic eEF1Balpha subunit show even greater resistance to CdSO(4), with or without eEF1Bgamma present [14].
• A Saccharomyces cerevisiae cDNA homologue of the elongation factor EF-1 beta was found among the clones obtained by immunoscreening of a yeast cDNA expression library with an antibody against calmodulin affinity-purified proteins [9].

Analytical, diagnostic and therapeutic context of EFB1

• Molecular cloning and characterization of a Candida albicans gene (EFB1) coding for the elongation factor EF-1 beta [7].
• Crystallization of the yeast elongation factor complex eEF1A-eEF1B alpha [1].

References