Q.Describe the process of translation in protein synthesis.
Translation converts the codon sequence of mRNA into a polypeptide, in three stages -- initiation, elongation and termination -- using tRNAs to deliver amino acids at the ribosome.
Step 1. Initiation: The small ribosomal subunit binds the mRNA near its 5' end; the initiator tRNA, carrying methionine (or formyl-methionine in prokaryotes), base-pairs its anticodon (UAC) with the initiation codon AUG. The large subunit then joins (requiring Mg2+ ions), positioning the initiator tRNA in the ribosome's P site while the A site remains vacant.
Step 2. Elongation -- codon recognition: A charged aminoacyl-tRNA carrying the next amino acid enters the vacant A site, its anticodon pairing with the exposed mRNA codon.
Step 3. Elongation -- peptide bond formation: The amino acid on the P-site tRNA is joined to the amino acid on the A-site tRNA by a peptide bond, a reaction catalysed by the ribosome's own ribozyme (peptidyl transferase) activity; the now-uncharged tRNA is released from the P site.
Step 4. Elongation -- translocation: The ribosome moves one codon along the mRNA, shifting the peptidyl-tRNA from the A site to the P site and ejecting the previous, discharged tRNA via the E site, so a new A site is exposed for the next incoming tRNA; this three-step cycle repeats, adding one amino acid roughly every 0.1 second.
Step 5. Termination: When a stop codon (UAA, UAG or UGA) enters the A site, no tRNA recognises it; instead a release factor binds the stop codon, the completed polypeptide is released into the cytoplasm, and the two ribosomal subunits dissociate along with the last tRNA and the mRNA.
Translation proceeds through initiation (small subunit + initiator tRNA at AUG, then large subunit joining), repeated elongation cycles (codon recognition, peptide-bond formation, translocation), and termination (release-factor-mediated release of the polypeptide at a stop codon).
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