Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

作者：Imkamp Frank; Striebel Frank; Sutter Markus; Oezcelik Dennis; Zimmermann Natalie; Sander Peter; Weber Ban Eilika^*

来源：EMBO Reports, 2010, 11(10): 791-797.

DOI：10.1038/embor.2010.119

• Dop
• depupylation
• pupylation
• proteasome
• Mpa

Post-translational modification of proteins with prokaryotic ubiquitin-like protein (Pup) is the bacterial equivalent of ubiquitination in eukaryotes. Mycobacterial pupylation is a two-step process in which the carboxy-terminal glutamine of Pup is first deamidated by Dop (deamidase of Pup) before ligation of the generated gamma-carboxylate to substrate lysines by the Pup ligase PafA. In this study, we identify a new feature of the pupylation system by demonstrating that Dop also acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes Pup from substrates by specific cleavage of the isopeptide bond. Depupylation can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa.

• 出版日期2010-10
• 单位河北医科大学