The prokaryotic ubiquitin-like protein presents poor cleavage sites for proteasomal degradation

Abstract

The prokaryotic ubiquitin-like protein presents poor cleavage sites for proteasomal degradation Graphical abstract Highlights d Pup, the bacterial ubiquitin analog, lacks favorable proteasome cleavage sites d Pup can escape the proteasome conjugated to a targetderived degradation fragment d Dop, a depupylase, efficiently removes the degradation fragment from Pup d Dop activity facilitates Pup recycling and re-conjugation to a new target

Degradation Mechanism of AAA+ Proteases and Regulation of Streptomyces Metabolism

“…Finally, these authors used the molecular mass of covalent modification to identify a Pup substrate (SHJG_3659) [ 77 ]. The depupylation function of Dop has also been confirmed in other microorganisms and is not explored further in this study [ 78 , 79 ]. When Pup is deamidated, it will hydrolyze ATP under the action of PafA and catalyze the phosphorylation of Glu [ 80 ], forming an intermediate that is connected to the substrate Lys [ 81 ].…”