Eukaryotic translation termination factor 1 (eRF1)

Eukaryotic translation termination factor 1 (eRF1) is an essential protein involved in the recognition of stop codons (UAA, UAG, UGA) during mRNA translation, and catalyzes the release of newly synthesized polypeptides from the ribosome. eRF1 functions as part of a complex with eRF3 and GTP, and is required for accurate termination of translation and for nonsense-mediated mRNA decay (NMD), which eliminates mRNAs with premature stop codons. The structure of eRF1 consists of three domains that collectively mimic tRNA, allowing eRF1 to fit into the ribosomal A-site and interact with the peptidyl transferase center to hydrolyze peptidyl-tRNA. Proper functioning of eRF1 is critical for cellular viability, with mutations in key motifs (such as the GGQ loop) leading to loss of function and cell death. eRF1 is highly conserved among eukaryotes and has functional homologs in archaea, with distinct evolutionary differences from prokaryotic release factors[1][2][3].

Other names

TB3-1SUP45L1ETF1ERF1