7.3.1

Translation

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Translation

Translation is the second step in protein synthesis. The steps involved are initiation, elongation, and termination. The process requires a lot of metabolic energy.

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Location of translation

  • mRNA that has been produced during transcription binds to a ribosome in the cytoplasm.
  • The ribosome is the site of protein synthesis.
    • In eukaryotes, ribosomes can also be found attached to the rough endoplasmic reticulum. So, translation can happen there too.
  • In prokaryotes, both transcription and translation occur in the cytoplasm. This means both processes occur simultaneously.
    • The newly formed mRNA molecule binds to a ribosome while the gene is still being transcribed.
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Initiation

  • Translation begins when the start codon of an mRNA molecule binds to the rRNA of a ribosome.
    • The start codon is almost always AUG.
  • Six bases (two codons) can fit inside the ribosome at one time.
  • One molecule of tRNA binds to the first codon in the ribosome.
  • The tRNA molecule has an anticodon that is complementary to a specific codon.
  • The anticodon allows the correct tRNA molecule to bind to the correct codon.
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Elongation

  • The large ibosomal consists of three compartments:
    • The A (aminoacyl) site binds incoming charged aminoacyl tRNAs.
    • The P (peptidyl) site binds charged tRNAs carrying amino acids that have formed peptide bonds with the growing polypeptide chain, but have not yet dissociated from their corresponding tRNA.
    • The E (exit) site releases dissociated tRNAs so that they can be recharged with free amino acids
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Elongation - 2

  • During translation elongation, the ribosome moves along the mRNA and ensures correct binding of mRNA codons to complementary tRNA anticodons.
  • Elongation proceeds with charged tRNAs entering the A site and then shifting to the P site followed by the E site with each single-codon “step” of the ribosome.
    • Ribosomal steps are induced by conformational changes that advance the ribosome by three bases in the 3' direction.
  • The energy for each step of the ribosome is donated by an elongation factor that hydrolyzes GTP.
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Elongation - peptide bond

  • Peptide bonds form between the amino group of the amino acid attached to the A-site tRNA and the carboxyl group of the amino acid attached to the P-site tRNA.
    • The formation of each peptide bond is catalyzed by peptidyl transferase.
  • The amino acid bound to the P-site tRNA is also linked to the growing polypeptide chain.
  • As the ribosome steps across the mRNA, the former P-site tRNA enters the E site, detaches from the amino acid, and is expelled.
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Termination

  • Termination of translation occurs when a nonsense codon (UAA, UAG, or UGA) is encountered.
  • Upon aligning with the A site, these nonsense codons are recognized by release factors in prokaryotes and eukaryotes.
  • These factors instruct peptidyl transferase to add a water molecule to the carboxyl end of the P-site amino acid.
    • This reaction forces the P-site amino acid to detach from its tRNA, and the newly made protein is released.
  • The ribosome detaches from the mRNA.
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Genetic code

  • The genetic code is a triplet code, with each RNA codon consisting of three consecutive nucleotides that specify one amino acid.
    • For example, the mRNA codon CAU specifies the amino acid histidine.
  • The code is degenerate; that is, some amino acids are specified by more than one codon.
    • For example, CCU and CCG are both codons for proline.
  • The same genetic code is universal to almost all organisms on Earth, providing for the common ancestry of life on earth.

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