Depupylase Dop Regulates Substrate Selectivity in Mycobacterium tuberculosis

Mycobacteria encode a prokaryotic ubiquitin-like protein that posttranslationally modifies proteins to mark them for proteolysis. Pupylation occurs on lysines of targeted proteins and is catalyzed by the ligase PafA. Like ubiquitylation, pupylation can be reversed by the depupylase Dop, which shares high structural similarity with PafA. Unique to Dop near its active site is a disordered loop of approximately 40 amino acids that is highly conserved among diverse dop-containing bacterial genera. Therefore, this study deleted discrete sequences from the Dop loop and assessed pupylation in mutant strains of Mycobacterium tuberculosis to understand the function of this domain. The dataset contains proteomic data, which suggest that these conserved amino acids play a role in substrate selectivity for Dop.