Reference - PMID:34019809 - Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
Reference summary
- PubMed ID
- PMID:34019809
- Title
- Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
- Authors
- Deng S, Gottlieb L, Pan B, Supplee J, Wei X, Petersson EJ, Marmorstein R
- Citation
- Structure 2021 Oct 07;29(10):1094-1104.e4
- Publication year
- 2021
- Abstract
- Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP 6 ), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP 6 binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP 6 -mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE.
