N-terminal acetylation of cellular proteins creates specific degradation signals.

@article{Hwang2010NterminalAO,
  title={N-terminal acetylation of cellular proteins creates specific degradation signals.},
  author={Cheol-Sang Hwang and Anna Shemorry and Alexander Varshavsky},
  journal={Science},
  year={2010},
  volume={327 5968},
  pages={
          973-7
        }
}
The retained N-terminal methionine (Met) residue of a nascent protein is often N-terminally acetylated (Nt-acetylated). Removal of N-terminal Met by Met-aminopeptidases frequently leads to Nt-acetylation of the resulting N-terminal alanine (Ala), valine (Val), serine (Ser), threonine (Thr), and cysteine (Cys) residues. Although a majority of eukaryotic proteins (for example, more than 80% of human proteins) are cotranslationally Nt-acetylated, the function of this extensively studied… CONTINUE READING

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