Ubiquitin-Specific E. coli Proteinase Does Not Require the Obligatory Presence of Dipeptide GlyGly at Processing Site

Abstract It is shown that, unlike eukaryotic ubiquitin-specific proteinases (deubiquitinating enzymes, DUBs), the E. coli deubiquitinase ElaD can process sites containing not only GlyGly but also GlyAla with equal efficiency. At the same time, the bacterial enzyme, like eukaryotic DUBs, fails to process sites containing AlaGly, AlaAla, or GlyPro dipeptides. In light of the functional mission of the E. coli deubiquitinating agent, its decreased specificity can be considered a valuable evolutional acquisition that allows expansion of the list of molecular targets attacked during pathogenesis.