Practice question

The functional eukaryotic counterpart of bacterial EF-Tu is eEF1A, also designated EEF1A1, a highly abundant GTP-binding protein. Like EF-Tu, eEF1A binds GTP and aminoacyl-tRNA to create a ternary complex that samples the A-site of the 80S ribosome during elongation cycles. Cognate codon recognition in the decoding center activates GTP hydrolysis, releasing eEF1A-GDP, which is recycled by the multisubunit eEF1B complex analogous to bacterial EF-Ts exchange factor. eEF1A is extremely abundant and highly conserved, reflecting its central role in translation. eEF2 corresponds to EF-G translocase, while eIF2 and eIF5B drive initiation rather than elongation tRNA delivery mechanisms.