Identification and characterization of the human ARD1-NATH protein acetyltransferase complex.

@article{Arnesen2005IdentificationAC,
  title={Identification and characterization of the human ARD1-NATH protein acetyltransferase complex.},
  author={Thomas Arnesen and Dave W. Anderson and Christian Baldersheim and Michel Lanotte and Jan Erik Varhaug and Johan Richard Lillehaug},
  journal={The Biochemical journal},
  year={2005},
  volume={386 Pt 3},
  pages={
          433-43
        }
}
Protein acetyltransferases and deacetylases have been implicated in oncogenesis, apoptosis and cell cycle regulation. Most of the protein acetyltransferases described acetylate epsilon-amino groups of lysine residues within proteins. Mouse ARD1 (homologue of yeast Ard1p, where Ard1p stands for arrest defective 1 protein) is the only known protein acetyltransferase catalysing acetylation of proteins at both alpha-(N-terminus) and epsilon-amino groups. Yeast Ard1p interacts with Nat1p (N… CONTINUE READING
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