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first step of polypeptide chain elongation
eEF1a binds GTP and an aa-tRNA: a ternary complex is formed
second step of polypeptide chain elongation
the codon at the A site recruits the complementary aa-tRNA-eEF1a-FTP complex
third step of polypeptide chain elongation
correct codon-anticodon pairing induces hydrolysis of GTP by eEF1a; this leads to conformaiton change in the ribosome, and th eeEF1a is released
fourth step of polypeptide chain elongation
in the new conformation state of the ribosome, the two aa-tRNAs are close to each other and the large rRNA catalyzes the formation of the peptide bond using the energy stored in the ester bond of the aa-tRNA at the P site
fifth step of polypeptide chain elongation
the 80S complex binds eEF2-GTP. The GTP is hydrolyzed by EF2 and this provides the energy for translocation: the ribosome moves “forward” by 3 bases and tRNA ends up in the E site. Now, the dipeptidyl-tRNA is at the P site, the ribosome is ready to by the next ternary complex at the A site