Here, the translation context effect is clearly seen as a strategic influence of distant mRNA codons on the inclusion (or non-inclusion) of certain amino acids in the composition of a protein being synthesized.
The amino acids are joined to form proteins by peptide bonds. The formation of peptide bonds requires a good amount of energy. Therefore, in the first phase of translation for protein synthesis, the amino acids are activated in the presence of ATP and linked to their cognate tRNA (transfer RNA). This process is called as charging of the tRNA or aminoacylation of tRNA. If two such charged tRNA are brought close enough, the formation of peptide bond between them is favored energetically. This function occurs inside the , as it contains two sites for subsequent amino acids to bind to and thus be close enough for bonding.
Protein Synthesis Scavenger Hunt Activity
For initiation of the translation process, the ribosome binds to the mRNA at the start codon recognized by the initiator tRNA. The ribosome then proceeds to the elongation phase of protein synthesis. During this stage, the complexes formed by amino acids are linked to tRNA, sub sequentially to bind to the appropriate codon in mRNA by forming complimentary base pairs with the tRNA anticodon. The ribosome moves from codon to codon along the mRNA. Amino acids are added one by one, translated into polypeptide sequences dictated by the DNA and represented by mRNA. At the end, release factor binds to the stop codon, thus terminating the translation stage and completing the protein synthesis process. The complete polypeptide is released from the .