3.3 Reading Resource : #3 The Process of Protein Synthesis Just as with mRNA synthesis, Protein synthesis has three stages: initiation, elongation, and termination.
The translation process is similar in prokaryotes and eukaryotes. In this section, we will look at how translation
works in E. coli, a representative prokaryote, and distinguish between prokaryotic and eukaryotic translation.
The formation of an initiation complex is the first step in the synthesis of proteins. This complex is
involved in E. coli by the small ribosome subunit, the mRNA template, three initiation factors, and a special
initiator tRNA. The initiator tRNA interacts with the AUG start codon, and links to a special form of the amino
acid methionine that is typically removed from the polypeptide after translation is complete.
In prokaryotes and eukaryotes, the basics of polypeptide elongation are the same, so we will review
elongation from the perspective of E. coli. The large ribosomal subunit of E. coli consists of three
compartments: The A site binds incoming charged tRNAs (tRNAs with their attached specific amino acids).
The P site binds charged tRNAs containing amino acids that have formed bonds with the growing polypeptide
chain but have not yet separated from their corresponding tRNA. The E site dissociates tRNAs, allowing them
to be recharged with free amino acids. The ribosome shifts one codon at a time, catalyzing each of the three
processes. A charged tRNA enters the complex with each step, the polypeptide grows by one amino acid, and
an uncharged tRNA exits. The energy for each bond between amino acids is derived from GTP, a molecule
similar to ATP (Figure 49). Surprisingly, the E. Each amino acid is added to the coli translation apparatus in
less than 0.05 seconds, implying that a 200-amino acid polypeptide could be translated in less than 10 seconds.
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Fowler, S.,Roush, R. & Wise, J. (2017)
Concepts in Biology, Chapter 9, -Pp. 213-214 OpenStax,
https://openstax.org/details/books/concepts-biology
,