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EMBO Rep. 2010 Oct;11(10):791-7. doi: 10.1038/embor.2010.119. Epub 2010 Aug 27.

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

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Department of Biology, Eidgenössische Technische Hochschule Zurich, Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, Zurich CH-8093, Switzerland.


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.

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