Loading of the initiator tRNA is the part of initiation of translation process.

Explanation: The events controlling the correct addition of amino acid are controlled by 3 proteins known as elongation factors. They are IF1, IF2 and IF3.

Explanation: The auxillary protein required for the elongation of polypeptide is energy dependent processes. All these factors use energy of the GTP binding and hydrolysis to enhance the rate and accuracy of ribosome function.

Explanation: Aminoacyl-tRNAs do not bind to the ribosome on their own. Instead, they are escorted to the ribosome by the elongation factor EF-Tu.

Explanation: Once the tRNA is aminoacylated, EF-Tu binds to the tRNA at the3’ end of the tRNA, masking the coupled amino acid. This interaction prevents the bound aminoacyl-tRNA from participating in peptide bond formation until it is released from EF-Tu.

Explanation: The trigger h the factor binding center after the tRNA is loaded into that activates the EF-Tu GTPase id known as factor binding center. EF-Tu only interacts with the factor binding center after the tRNA is loaded into the A site and a correct codon-anticodon match is made. At this point, EF-Tu hydrolyzed its bound GTP and is released from the ribosome.

Explanation: The energy difference between a correctly formed codon-anticodon pair and that of a near match is not equal but still cannot account for the high level of accuracy required for the translation process. Thus there are three more mechanisms that contribute to this specificity. In each case, these mechanisms select against incorrect codon-anticodon pairings.

Explanation: A total of 4 mechanisms are involved in the maintenance of the fidelity of translation. In addition to the codon-anticodon interactions, the ribosome exploits minor grove interactions and two phases of proof reading to ensure that a correct aminoacyl-tRNA binds in the A site.

Explanation: Once the correctly charged tRNA has been placed in the A site and has rotated into the peptidyl transferase center, peptide bond formation takes place. This reaction is catalyzed by RNA, specifically the 23S rRNA component of the large subunit.

Explanation: For a new round of peptide chain elongation to occur, the P site tRNA must move to the E site and the A site tRNA must move to the P site. At the same time, the mRNA must move by 3 nucleotides to expose the next codon. These movements are coordinated within the ribosome and are collectively referred to as translocation.

Explanation: The completion of translocation requires the action of a second elongation factor called EF-G. EF-G can only bind to the ribosome when associated with GTP. After the peptidyl transferase reaction, the shift in the location of the A site tRNA uncovers a binding site for EF-G in the large subunit portion of the A site.