Protein synthesis terminates when the ribosome translocates to a termination codon. Because there are no tRNAs with anticodons complementary to the termination codons, no tRNA enters the A site of the ribosome when a termination codon is encountered (Figure 15.23a). Instead, proteins called release factors bind to the ribosome (Figure 15.23b). E. coli has three release factors—RF^ RF2, and RF3. Release factor 1 recognizes the termination codons UAA and UAG, and RF2 recognizes UGA and UAA. Release factor 3 forms a complex with GTP and binds to the ribosome. The release factors then promote the cleavage of the tRNA in the P site from the polypeptide chain; in the process, the GTP that is complexed to RF3 is hydrolyzed to GDP. Additional factors help bring about the release of the tRNA from the P site, the release of the mRNA from the ribosome, and the dissociation of the ribosome (Figure 15.23c). Translation in eukaryotic cells terminates in a similar way, except that there are two release factors: eRF1, which recognizes all three termination codons, and eRF2, which binds GTP and stimulates the release of the polypeptide from the ribosome.

Findings from recent studies suggest that the release factors bring about the termination of translation by completing a final elongation cycle of protein synthesis. In this model, RFj and RF2 are similar in size and shape to tRNAs and occupy the A site of the ribosome, just as the amino acid - tRNA - EF - Tu - GTP complex does during an elongation cycle. Release factor 3 is structurally similar to EF-G; it then translocates RF1 and RF2 to the P site, as well as the last tRNA to the E site, in a way similar to that in which EF-G brings about translocation. When both the A site and the P site of the ribosome are cleared of tRNAs, the ribosome can dissociate. Research findings also indicate that some of the sequences in the rRNA play a role in the recognition of termination codons.

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