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Background  Protein acetylation is among the most common protein modifications. The two major types are post-translational N ε -lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone acetyltransferases) and co-translational N α -terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The major NAT complex in yeast, NatA, is composed of the catalytic subunit Naa10p ( N a lpha  a cetyltransferase  10 p rotein) (Ard1p) and the auxiliary subunit Naa15p (Nat1p). The NatA complex potentially acetylates Ser-, Ala-, Thr-, Gly-, Val- and Cys- N-termini after Met-cleavage. In humans, the homologues hNaa15p (hNat1) and hNaa10p (hArd1) were demonstrated to form a stable ribosome associated NAT complex acetylating NatA type N-termini  in vitro  and  in vivo .    Results  We here describe a novel human protein, hNaa16p (hNat2), with 70% sequence identity to hNaa15p (hNat1). The gene encoding hNaa16p originates from an early vertebrate duplication event from the common ancestor of h NAA15  and h NAA16 . Immunoprecipitation coupled to mass spectrometry identified both endogenous hNaa15p and hNaa16p as distinct interaction partners of hNaa10p in HEK293 cells, thus demonstrating the presence of both hNaa15p-hNaa10p and hNaa16p-hNaa10p complexes. The hNaa16p-hNaa10p complex acetylates NatA type N-termini  in vitro . hNaa16p is ribosome associated, supporting its potential role in cotranslational N α -terminal acetylation. h NAA16  is expressed in a variety of human cell lines, but is generally less abundant as compared to h NAA15 . Specific knockdown of h NAA16  induces cell death, suggesting an essential role for hNaa16p in human cells.    Conclusion  At least two distinct NatA protein N α -terminal acetyltransferases coexist in human cells potentially creating a more complex and flexible system for N α -terminal acetylation as compared to lower eukaryotes.

A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)