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.
Full text not available from this repository.
View at publisher
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|
|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|
Users (please log in): suggest update or correction for this item
Repository Staff Only: item control page