Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway.
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.
Imkamp
Frank
F
Department of Biology, Eidgenössische Technische Hochschule Zurich, Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, Zurich CH-8093, Switzerland.
Striebel
Frank
F
Sutter
Markus
M
Ozcelik
Dennis
D
Zimmermann
Natalie
N
Sander
Peter
P
Weber-Ban
Eilika
E
D001426:Bacterial Proteins / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000235:genetics / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014452:Ubiquitins / Q000378:metabolism*
D001426:Bacterial Proteins; C533288:Pup protein, Mycobacterium tuberculosis; D014452:Ubiquitins; D005973:Glutamine; D046988:Proteasome Endopeptidase Complex; D008025:Ligases; D008239:Lysine
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