LAUSR

Histone acetylation involves the addition of acetyl groups to specific amino acid residues. This chemical histone modification is broadly divided into two types - acetylation of the amino group found on the side chain of internal lysine residues (lysine acetylation) or acetylation of the α-amino group at the N-terminal amino acid residue (N-terminal acetylation). Although the former modification is considered a classic epigenetic mark, the biological importance of N-terminal acetylation has been mostly overlooked in the past, despite its widespread occurrence and evolutionary conservation. However, recent studies have now conclusively demonstrated that histone N-terminal acetylation impacts important cellular processes, such as controlling gene expression and chromatin function, and thus ultimately affecting biological phenotypes, such as cellular ageing, metabolic rewiring and cancer. In this Review, we provide a summary of the literature, highlighting current knowledge on the function of this modification, as well as allude to open questions we expect to be the focus of future research on histone N-terminal acetylation.