Reaction: (1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nα-acetyl-L-seryl-[histone H4] + CoA
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nα-acetyl-L-seryl-[histone H2A] + CoA
Other name(s): NAA40 (gene name)
Systematic name: acetyl-CoA:N-terminal-L-seryl-[histone 4/2A] L-serine Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Song, O.K., Wang, X., Waterborg, J.H. and Sternglanz, R. An Nα-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J. Biol. Chem. 278 (2003) 38109-38112. [PMID: 12915400]
2. Polevoda, B., Hoskins, J. and Sherman, F. Properties of Nat4, an Nα-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. Mol. Cell Biol. 29 (2009) 2913-2924. [PMID: 19332560]
3. Magin, R.S., Liszczak, G.P. and Marmorstein, R. The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. Structure 23 (2015) 332-341. [PMID: 25619998]