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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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Abstract

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.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Medical Microbiology
DDC:570 Life sciences; biology
610 Medicine & health
Date:2010
Deposited On:24 Jan 2011 15:23
Last Modified:27 Nov 2013 23:08
Publisher:Nature Publishing Group
ISSN:1469-221X
Publisher DOI:10.1038/embor.2010.119
PubMed ID:20798673
Citations:Web of Science®. Times Cited: 21
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Scopus®. Citation Count: 24

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