Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection.
In: eLife, 2020-11-26, S. 1-21
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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 A°. 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. [ABSTRACT FROM AUTHOR]
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Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection.
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Autor/in / Beteiligte Person: | Shin, Donghyuk ; Bhattacharya, Anshu ; Cheng, Yi-Lin ; Alonso, Marta Campos ; Mehdipour, Ahmad Reza ; van der Heden van Noort, Gerbrand J. ; Ovaa, Huib ; Hummer, Gerhard ; Dikic, Ivan |
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Zeitschrift: | eLife, 2020-11-26, S. 1-21 |
Veröffentlichung: | 2020 |
Medientyp: | academicJournal |
ISSN: | 2050-084X (print) |
DOI: | 10.7554/eLife.58277 |
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