Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases

Mol Cell. 2019 Mar 21;73(6):1097-1114. doi: 10.1016/j.molcel.2019.02.007. Epub 2019 Mar 13.


Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For instance, the identification of Golgi- and chloroplast-associated NATs shows that acetylation of N termini also happens post-translationally. In addition, we now appreciate that some NATs are highly specific; for example, a dedicated NAT responsible for post-translational N-terminal acetylation of actin was recently revealed. Other studies have extended NAT function beyond Nt acetylation, including functions as lysine acetyltransferases (KATs) and non-catalytic roles. Finally, emerging studies emphasize the physiological relevance of N-terminal acetylation, including roles in calorie-restriction-induced longevity and pathological α-synuclein aggregation in Parkinson's disease. Combined, the NATs rise as multifunctional proteins, and N-terminal acetylation is gaining recognition as a major cellular regulator.

Keywords: KAT; N-terminal acetylation; N-terminal acetyltransferase; NAA10; NAA80; NAT; acetylation; actin; lysine acetyltransferase; protein modifications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Catalysis
  • Humans
  • N-Terminal Acetyltransferases / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Domains
  • Protein Processing, Post-Translational*
  • Proteolysis
  • Signal Transduction
  • Substrate Specificity


  • N-Terminal Acetyltransferases
  • Proteasome Endopeptidase Complex