Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.

ABSTRACT: The heterotrimeric NatC complex, comprising the catalytic Naa30 and the two auxiliary subunits Naa35 and Naa38, co-translationally acetylates the N-termini of numerous eukaryotic target proteins. Despite its unique subunit composition, its essential role for many aspects of cellular function and its suggested involvement in disease, structure and mechanism of NatC have remained unknown. Here, we present the crystal structure of the Saccharomyces cerevisiae NatC complex, which exhibits a strikingly different architecture compared to previously described N-terminal acetyltransferase (NAT) complexes. Cofactor and ligand-bound structures reveal how the first four amino acids of cognate substrates are recognized at the Naa30-Naa35 interface. A sequence-specific, ligand-induced conformational ch

SUBMITTER: Grunwald S 

PROVIDER: S-EPMC7608589 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature