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EF-G catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation. [1] In this process, the peptidyl transferase center (PTC) has catalyzed the formation of a peptide bond between amino acids, moving the polypeptide chain from the P site tRNA to the A site tRNA.
Termination of elongation depends on eukaryotic release factors. The process is similar to that of bacterial termination, but unlike bacterial termination, there is a universal release factor, eRF1, that recognizes all three stop codons. Upon termination, the ribosome is disassembled and the completed polypeptide is released. eRF3 is a ribosome ...
Elongation is the most ... Elongation factors play a role in orchestrating the events of this process, ... catalyzes the translocation of the tRNA and mRNA down the ...
In the final stage of elongation, called translocation, the deacylated tRNA (in the P site) and the dipeptidyl-tRNA (in the A site) along with its corresponding codons move to the E and P sites, respectively, and a new codon moves into the A site. This process is catalyzed by elongation factor G (EF-G).
Elongation: The last tRNA validated by the small ribosomal subunit (accommodation) transfers the amino acid. It carries to the large ribosomal subunit which binds it to one of the preceding admitted tRNA (transpeptidation). The ribosome then moves to the next mRNA codon to continue the process (translocation), creating an amino acid chain.
EC 7.2.1 Translocation of inorganic cations linked to oxidoreductase reactions; EC 7.2.2 Translocation of inorganic cations linked to the hydrolysis of a nucleoside triphosphate; EC 7.2.4 Translocation of inorganic cations linked to decarboxylation; An important translocase contained in this group is Na+/K+ pump, also known as EC 7.2.2.13.
Then, in a process catalyzed by the prokaryotic elongation factor EF-G (historically known as translocase), the coordinated translocation of the tRNAs and mRNA occurs, with the P-site tRNA moving to the E-site, where it dissociates from the ribosome, and the A-site tRNA moves to take its place in the P-site. [6] [7]
Due to the fact that translation elongation is an irreversible process, there are few known mechanisms of its regulation. However, it has been shown that translational efficiency is reduced via diminished tRNA pools, which are required for the elongation of polypeptides.