The ribosome-associated N-terminal acetyltransferase A regulates proteome stability in plants

N-terminal acetylation is one of the most common protein modifications in eukaryotes. The NatA complex is the dominant regulator of the N-acetylome in all eukaryotes. Here, we show that the imprinting of the proteome with acetylation marks by the essential NatA complex is a critical trigger for stabilizing plant proteins. Depleting 70% of the NatA activity by downregulation of the catalytic or the ribosome anchoring subunit causes 4-fold faster degradation of total proteins in Arabidopsis. This proteome dataset compares the NatA depleted Arabidopsis lines amiNAA10 and amiNAA15 to wild type Arabidopsis.