The alpha subunit of elongation factor-1 (EEF1A) is involved in the binding of aminoacyl-tRNAs to 80S ribosomes. During the process, GTP is hydrolyzed into GDP. To perform this function, EEF1A has domains th at bind guanine nucleotides, 80S ribosomes, and aminoacyl-tRNAs. Also, EEF1A interacts with the beta subunit of EEF1 to exchange bound GDP for GTP. Multimolecular complexes involving the eukaryotic elongation factor 1A (eEF1A) have been suggested to play an important role in the channeling (vectorial transfer) of tRNA during protein synthesis HIV-1 matrix protein (MA) was found to interact with elongation factor 1-α (EF1α), an essential component of the translation machinery th at delivers aminoacyl-tRNA to ribosomes. The interaction between MA and EF1α impairs translation in vitro, a result consistent with a previously proposed model in which inhibition of translation by the accumulation of Gag serves to release viral RNA from polysomes, permitting the RNA to be packaged into nascent virions. It has been identified th at the translation elongation factor, eEF1A, and its guanine nucleotide exchange factor, eEF1Bβ, as translationally controlled tumor protein (TCTP)-interacting partners.
