page_title: Acetylation
section_title: NatA
hierarchical_section_title: Acetylation / Protein acetylation / N-terminal acetylation / N-terminal acetyltransferases / NatA
caption_attribution_description: English: Crystal structure of NatA complex from Schizosaccharomyces pombe. Naa10 is shown in cyan and Naa15 is shown in green. (PDB ID: 4KVM)
context_page_description: Acetylation describes a reaction that introduces an acetyl functional group into a chemical compound. Deacetylation is the removal of an acetyl group.
  Acetylation refers to the process of introducing an acetyl group into a compound, namely the substitution of an acetyl group for an active hydrogen atom. A reaction involving the replacement of the hydrogen atom of a hydroxyl group with an acetyl group yields a specific ester, the acetate. Acetic anhydride is commonly used as an acetylating agent reacting with free hydroxyl groups. For example, it is used in the synthesis of aspirin, heroin, and THC-O-acetate.
context_section_description: NatA is composed of two subunits, the catalytic subunit Naa10 and the auxiliary subunit Naa15. NatA subunits are more complex in higher eukaryotes than in lower eukaryotes. In addition to the genes NAA10 and NAA15, the mammal-specific genes NAA11 and NAA16, make functional gene products, which form different active NatA complexes. Four possible hNatA catalytic-auxiliary dimers are formed by these four proteins. However, Naa10/Naa15 is the most abundant NatA.
  NatA acetylates Ser, Ala-, Gly-, Thr-, Val- and Cys N-termini after the initiator methionine is removed by methionine amino-peptidases. These amino acids are more frequently expressed in the N-terminal of proteins in eukaryotes, so NatA is the major NAT corresponding to the whole number of its potential substrates.
  Several different interaction partners are involved in the N-terminal acetylation by NatA. Huntingtin interacting protein K (HYPK) interacts with hNatA on the ribosome to affect the N-terminal acetylation of a subset of NatA substrates. Subunits hNaa10 and hNaa15 will increase the tendency for aggregation of Huntingtin if HYPK is depleted. Hypoxia-inducible factor (HIF)-1α has also been found to interact with hNaa10 to inhibit hNaa10-mediated activation of β-catenin transcriptional activity.
caption: Crystal structure of the NatA complex (Naa10 and Naa15) from Schizosaccharomyces pombe. The green chains represent the auxiliary subunit Naa15 and the cyan chains the catalytic subunit Naa10.[8] (PDB ID: 4KVM)
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