About: Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection

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About: Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
Creator	Ovaa, Huib Dikic, Ivan Van Der Heden Van Noort, Gerbrand Bhattacharya, Anshu Campos Alonso, Marta »more»
source	BioRxiv
abstract	Legionella pneumophila is a gram-negative pathogenic bacterium that causes Legionaries’ disease. The Legionella genome codes more than 300 effector proteins able to modulate host-pathogen interactions during infection. Among them are also enzymes altering the host-ubiquitination system including bacterial ligases and deubiquitinases. In this study, based on homology-detection screening on 305 Legionella effector proteins, we identified two Legionella OTU-like deubiquitinases (LOT; LotB (Lpg1621/Ceg23) and LotC (Lpg2529), LotA (Lpg2248/Lem21) is already known). A crystal structure of LotC catalytic core (LotC14-310) was determined at 2.4 Å and compared with other OTU deubiquitinases, including LotB. Unlike the classical OTU-family, the structures of Legionella OTU-family (LotB and LotC) shows an extended helical lobe between the Cys-loop and the variable loop, which define a novel class of OTU-deubiquitinase. Despite structural differences in their helical lobes, both LotB and LotC interact with ubiquitin. LotB has an additional ubiquitin binding site (S1’) enabling specific cleavage of Lys63-linked poly-ubiquitin chains. By contrast, LotC only contains the S1 site and cleaves different species of ubiquitin chains. MS analysis of catalytically inactive LotB and LotC identified different categories of host-substrates for these two related DUBs. Together, our results provide new structural insights of bacterial OTU deubiquitinases and indicate distinct roles of bacterial deubiquitinases in host-pathogen interactions.
has issue date	2020-04-28(xsd:dateTime)
bibo:doi	10.1101/2020.04.25.060954
has license	biorxiv
sha1sum (hex)	1632e4e7b51e9401b93cdfd9bbdf300b78b8035c
schema:url	https://doi.org/10.1101/2020.04.25.060954
resource representing a document's title	Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
schema:publication	bioRxiv
resource representing a document's body	covid:1632e4e7b51e9401b93cdfd9bbdf300b78b8035c#body_text
is schema:about of	named entity 'ROLES' named entity 'ALTERING' named entity '300' named entity 'biochemical' named entity 'RPS27' »more»

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