Abstract 2027 Characterization of the metal-binding properties of arginyltransferase 1 (ATE1)

Arginyltransferase1 (ATE1) is a highly conserved eukaryotic enzyme that catalyzes a post-translational modification (PTM) known as arginylation. This critical PTM is involved in numerous biological processes such as stress regulation, nerve regeneration, neurodegeneration, and even protein degradation. ATE1 transfers an L-Arg moiety from an aminoacylated Arg-tRNAArg most commonly to the N-terminal of an acceptor protein in an ATP-independent, non-ribosomal manner. Our lab has determined the structure of the apo form of Saccharomyces cerevisiae ATE1 (ScATE1), revealing a bilobed architecture and the presence of a GCN5-related N-acetyltransferase (GNAT) active-site adjacent to a Cys-rich N-terminal regulatory domain.