Co-translational processing and modification are critical steps in protein synthesis, occurring simultaneously with translation. As the nascent polypeptide chain emerges from the ribosome, it undergoes various modifications that help ensure proper folding, localization, and function. Disturbances of correct co-translational processing leads to human diseases like cancer, neurodegenerative diseases or inflammatory disorders.
N-terminal acetylation (Nt-ac) is the most pervasive co-translational modification and 80% of all nascent human proteins receive an N-terminal acetyl group. Different functions in protein- protein stability, protein interactions and localization have been described, but many questions remain still open e.g. why the cell spends a huge amount of energy using acetyl-CoA as acetyl-CoA. We use CrispR/Cas9 technologies combined with quantitative proteomics to dissect the diverse roles of Nt-ac.