Elongation, a crucial step in the translation process of protein synthesis, gets disrupted by amino acid sequences with an abundance of N-terminal aspartic and glutamic acid residues in eukaryotic cells, discovered researchers from Tokyo Tech and University of Hyogo. The team's findings show that these "risky" amino acids can destabilize the ribosomal machinery. As a consequence, most proteomes tend to avoid incorporating them at the N-terminals of peptide sequences, indicating a bias in amino acid distribution.
Life depends on the precise functioning of several proteins synthesized in cells by ribosomes. This diverse set of proteins, known as a proteome, is maintained by the robust translation elongation of amino acid sequences taking place in the ribosomes. The translation mechanisms which ensure that nascent chains of polypeptides—long chains of amino acids—are elongated without getting detached are conserved in all living organisms. However, the rates of elongation are not constant. Elongation is often interrupted by interactions between positively charged nascent polypeptides and negatively charged ribosomal RNA.