Practice question

Eukaryotic termination employs two factors with distinct roles coordinated for release. eRF1 is a class I release factor that structurally mimics tRNA and enters the A-site, where its N-terminal domain recognizes UAA, UAG, and UGA stop codons via conserved TASNIKS and other motifs, providing omnipotent decoding unlike bacterial split systems. Its central domain bearing the methylated GGQ motif then catalyzes hydrolysis of peptidyl-tRNA ester bond in peptidyl transferase center. eRF3 is a GTPase that stimulates termination fidelity and recycling but does not decode stops. Bacterial RF1 and RF2 split codon specificity, contrasting with single eukaryotic factor approach.