Abstract 1634 A ribosome exchange factor for cotranslational N-terminal protein acetylation

Approximately 80% of mammalian proteins are acetylated at their N-terminus during translation. The function of N-terminally acetylated proteins can vary drastically from one protein to the next, resulting in changes to half-life, enabling new binding interactions, and altering the aggregation propensity of a protein. Interestingly, in contrast to e-lysine acetylation, N-terminal acetylation (NTA) is irreversible and is thus regulated in other ways. For example, N-terminal acetyltransferase A (NatA), which mediates 50% of all NTA, is tightly bound to the regulatory protein Huntingtin interacting protein K (HYPK).