Translation Elongation and Termination: 2 Are They Conserved Processes?

Eltschinger, Sandra; Bütikofer, Peter; Altmann, Michael (2016). Translation Elongation and Termination: 2 Are They Conserved Processes? In: Hernández, Greco; Jagus, Rosemary (eds.) Evolution of The Protein Synthesis Machinery and Its Regulation (pp. 277-311). Springer International 10.1007/978-3-319-39468-8_13

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Translation initiation is followed by a process in which sequential addition of amino acid residues enables peptide chain formation, called translation elongation. Elongation decodes the codons on an mRNA and depends on elongation factors (EFs). In a first step, a ternary complex consisting of EF1A/EF-Tu-GTP-aminoacyl-tRNA (aa-tRNA) is formed and the elongator aa-tRNA is recruited to the ribosomal acceptor (A-) site. Hydrolysis of EF1A/EF-Tu-GTP is activated upon codon-anticodon decoding at the A-site and mRNA-tRNA interaction with the ribosome. Subsequently, peptide bond formation occurs between the aa moiety of the A-site aa-tRNA and the peptidyl-tRNA located at the ribosomal peptidyl (P-) site. Thereafter, the deacylated tRNA is moved to the exit (E-) site [1–4]. This elongating process is repeated until a stop codon (UAA, UAG and UGA) is encountered. Exposing a stop codon at the A-site initiates the process of Translation termination. Polypeptide release factors mediate the release of the polypeptide chain from the ribosome by hydrolysis of the ester bond between the polypeptide chain and the tRNA at the P-site [1–3, 5].

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