<prompt> Please answer with one of the option in the bracket. Write reasoning in between . Write answer in between .Q:An investigator is studying the modification of newly formed polypeptides in plated eukaryotic cells. After the polypeptides are released from the ribosome, a chemically-tagged protein attaches covalently to lysine residues on the polypeptide chain, forming a modified polypeptide. When a barrel-shaped complex is added to the cytoplasm, the modified polypeptide lyses, resulting in individual amino acids and the chemically-tagged proteins. Which of the following post-translational modifications has most likely occurred?? A: Acylation, B: Glycosylation, C: Phosphorylation, D: Carboxylation, E: Ubiquitination,  <response>: This is a question about post-translational modifications of proteins. The key details in the question stem are:- A tagged protein attaches to lysine residues on a newly synthesized polypeptide after it is released from the ribosome. This indicates a covalent modification.- When a barrel-shaped complex is added, the modified polypeptide lyses into individual amino acids and the tagged proteins. This indicates that the modification targets the polypeptide for degradation.Based on these clues, it seems the modification is ubiquitination. Ubiquitin proteins become covalently attached to lysine residues of target proteins, marking them for degradation by the proteasome which is a barrel-shaped complex.E: Ubiquitination 