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Imkamp, F; Striebel, F; Sutter, M; Ozcelik, D; Zimmermann, N; Sander, P; Weber-Ban, E (2010). Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway. EMBO Reports, 11(10):791-797.

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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 γ-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.


34 citations in Web of Science®
38 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Medical Microbiology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Deposited On:24 Jan 2011 15:23
Last Modified:05 Apr 2016 14:27
Publisher:Nature Publishing Group
Publisher DOI:10.1038/embor.2010.119
PubMed ID:20798673

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