Nature Communications (Jun 2017)

Structural basis of HypK regulating N-terminal acetylation by the NatA complex

  • Felix Alexander Weyer,
  • Andrea Gumiero,
  • Karine Lapouge,
  • Gert Bange,
  • Jürgen Kopp,
  • Irmgard Sinning

DOI
https://doi.org/10.1038/ncomms15726
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 10

Abstract

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N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of NatA.