EEF2 Human

eEF2 is a member of the GTP-binding translation elongation factor family. It plays an essential role in the elongation phase of protein synthesis by promoting the GTP-dependent translocation of the ribosome along the mRNA. This translocation is a critical step that moves the ribosome from one codon to the next, allowing for the addition of amino acids to the growing polypeptide chain .

The human recombinant form of eEF2 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 308 amino acids (574-858) with a molecular mass of 34.3 kDa. It is fused to a 23 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques .

eEF2 undergoes several post-translational modifications, including the modification of a specific histidine residue to diphthamide. This modification is crucial for the protein’s function and is conserved across most archaea and eukaryotes .

The activity of eEF2 is tightly regulated by phosphorylation. eEF2 kinase (eEF2K) phosphorylates eEF2, leading to its inactivation. This regulation is essential for controlling protein synthesis in response to various cellular signals and stress conditions .

eEF2 is a target for certain bacterial toxins, such as diphtheria toxin from Corynebacterium diphtheriae and exotoxin A from Pseudomonas aeruginosa. These toxins inactivate eEF2 by ADP-ribosylation, leading to the inhibition of protein synthesis in the host cells and causing symptoms associated with the respective infections .

The recombinant form of eEF2 is widely used in research to study the mechanisms of protein synthesis and the regulation of translation elongation. It is also used in the development of therapeutic agents targeting the translation machinery for the treatment of various diseases, including cancer .