A newly discovered post-translational modification--the acetylation of serine and threonine residues

Trends Biochem Sci. 2007 May;32(5):210-6. doi: 10.1016/j.tibs.2007.03.007. Epub 2007 Apr 6.


Recent studies on a bacterial virulence factor, YopJ of Yersinia, have led to the realization that the acetylation of serine and threonine residues could be an important form of post-translational modification in eukaryotes. Although the identification of the machinery used for the addition and removal of acetyl groups on serine or threonine residues is in its infancy, the enzymes thus-far studied provide early insight into the mechanism of this newly discovered post-translational modification, and hint at its potential importance. For example, acetylation can compete with phosphorylation targeted to the same residues and could, therefore, alter the course of signaling pathways. What are the implications for signal transduction in eukaryotes and how widespread could acetylation of serine and threonine prove to be?

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Bacterial Proteins / metabolism
  • Models, Biological
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Serine / metabolism*
  • Threonine / metabolism*
  • Virulence Factors / metabolism
  • Yersinia / metabolism


  • Bacterial Proteins
  • Virulence Factors
  • YopP protein, Yersinia
  • Threonine
  • Serine