Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms

Sci Rep. 2016 Feb 10;6:21304. doi: 10.1038/srep21304.


Protein N-terminal acetylation is an ancient and ubiquitous co-translational modification catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). Prokaryotes have at least 3 NATs, whereas humans have six distinct but highly conserved NATs, suggesting an increase in regulatory complexity of this modification during eukaryotic evolution. Despite this, and against our initial expectations, we determined that NAT diversification did not occur in the eukaryotes, as all six major human NATs were most likely present in the Last Eukaryotic Common Ancestor (LECA). Furthermore, we also observed that some NATs were actually secondarily lost during evolution of major eukaryotic lineages; therefore, the increased complexity of the higher eukaryotic proteome occurred without a concomitant diversification of NAT complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Arabidopsis / enzymology*
  • Arabidopsis / metabolism
  • Biological Evolution*
  • Drosophila melanogaster / enzymology*
  • Drosophila melanogaster / metabolism
  • Eukaryotic Cells / enzymology*
  • Eukaryotic Cells / metabolism
  • Genetic Variation
  • Humans
  • N-Terminal Acetyltransferases / genetics*
  • Proteome / genetics
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / metabolism
  • Sequence Alignment


  • Proteome
  • N-Terminal Acetyltransferases