Reference - PMID:23912279 - Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
Reference summary
- PubMed ID
- PMID:23912279
- Title
- Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
- Authors
- Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R
- Citation
- Nat Struct Mol Biol 2013 Sep;20(9):1098-105
- Publication year
- 2013
- Abstract
- N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.
