Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
In: ELIFE eLife, Vol 9 (2020) eLife, 9. ELIFE SCIENCES PUBLICATIONS LTD eLife; (2020)
Online
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Zugriff:
Legionella pneumophila causes a severe pneumonia known as Legionnaires’ disease. During the infection, Legionella injects more than 300 effector proteins into host cells. Among them are enzymes involved in altering the host-ubiquitination system. Here, we identified two LegionellaOTU (ovarian tumor)-like deubiquitinases (LOT-DUBs; LotB [Lpg1621/Ceg23] and LotC [Lpg2529]). The crystal structure of the LotC catalytic core (LotC14-310) was determined at 2.4 Å. Unlike the classical OTU-family, the LOT-family shows an extended helical lobe between the Cys-loop and the variable loop, which defines them as a unique class of OTU-DUBs. LotB has an additional ubiquitin-binding site (S1’), which enables the specific cleavage of Lys63-linked polyubiquitin chains. By contrast, LotC only contains the S1 site and cleaves different species of ubiquitin chains. MS analysis of LotB and LotC identified different categories of host-interacting proteins and substrates. Together, our results provide new structural insights into bacterial OTU-DUBs and indicate distinct roles in host–pathogen interactions.
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Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
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Autor/in / Beteiligte Person: | Ovaa, Huib ; Dikic, Ivan ; Shin, Donghyuk ; Hummer, Gerhard ; Marta Campos Alonso ; Ahmad Reza Mehdipour ; Bhattacharya, Anshu ; Gerbrand J. van der Heden van Noort ; Yi Lin Cheng |
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Quelle: | ELIFE eLife, Vol 9 (2020) eLife, 9. ELIFE SCIENCES PUBLICATIONS LTD eLife; (2020) |
Veröffentlichung: | 2020 |
Medientyp: | unknown |
ISSN: | 2050-084X (print) |
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