Journal
EMBO REPORTS
Volume 11, Issue 10, Pages 791-797Publisher
WILEY
DOI: 10.1038/embor.2010.119
Keywords
Dop; depupylation; pupylation; proteasome; Mpa
Categories
Funding
- Swiss National Science Foundation (SNF)
- Eidgenossische Technische Hochschule
- Fonds der Chemischen Industrie
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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.
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