Molecular mechanism of N-terminal acetylation by the ternary NatC complex.

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 (IP₆), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP₆ binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP₆-mediated NatC complex stabilization and the overlapping yet d

SUBMITTER: Deng S 

PROVIDER: S-EPMC8500922 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature