NAC guides a ribosomal multienzyme complex for nascent protein processing.

ABSTRACT: Approximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), respectively¹. Both modifications are strictly cotranslational and essential in higher eukaryotic organisms¹. The interaction, activity and regulation of these enzymes on translating ribosomes are poorly understood. Here we perform biochemical, structural and in vivo studies to demonstrate that the nascent polypeptide-associated complex^2,3 (NAC) orchestrates the action of these enzymes. NAC assembles a multienzyme complex with MetAP1 and NatA early during translation and pre-positions the active sites of both enzymes for timely sequential processing of the nascent p

SUBMITTER: Lentzsch AM 

PROVIDER: S-EPMC12039536 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature