EEF1G Human

eEF1G is a multi-domain protein that includes a glutathione transferase (GST)-like N-terminus domain . This domain is believed to be involved in the regulation of the assembly of multisubunit complexes containing this elongation factor and aminoacyl-tRNA synthetases . The primary function of eEF1G is to facilitate the enzymatic delivery of aminoacyl-tRNAs to the ribosome during the elongation phase of protein synthesis .

The eEF1 complex, which includes eEF1G, is responsible for the accurate and efficient delivery of aminoacyl-tRNAs to the ribosome. This process is mediated by the hydrolysis of GTP, which provides the necessary energy for the elongation step of protein synthesis . eEF1G, in association with other subunits such as eEF1A, eEF1B, and eEF1D, forms a high-molecular-weight complex that ensures the proper functioning of the translation machinery .

Mutations or dysregulation of the EEF1G gene have been associated with various diseases, including chest wall lymphoma and Pontiac fever . The protein’s involvement in critical cellular processes makes it a potential target for therapeutic interventions in these conditions.

Recombinant human eEF1G is produced using recombinant DNA technology, which involves inserting the human EEF1G gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its function, interactions, and potential therapeutic uses.

Research on eEF1G has revealed its interactions with several other proteins, including eEF1B2, eEF1D, HARS, LZTS1, LARS, and RECQL5 . These interactions highlight the protein’s role in various cellular processes beyond protein synthesis, such as response to viral infections and glutathione metabolism .