Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection.
In: ELife, Jg. 9 (2020-11-13)
Online
academicJournal
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 L egionella OT U (ovarian tumor)-like deubiquitinases (LOT-DUBs; LotB [Lpg1621/Ceg23] and LotC [Lpg2529]). The crystal structure of the LotC catalytic core (LotC 14-310 ) 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.
Competing Interests: DS, AB, YC, MA, AM, Gv, HO, GH No competing interests declared, ID Reviewing editor, eLife
(© 2020, Shin et al.)
| Titel: |
Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection.
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| Autor/in / Beteiligte Person: | Shin, D ; Bhattacharya, A ; Cheng, YL ; Alonso, MC ; Mehdipour, AR ; van der Heden van Noort GJ ; Ovaa, H ; Hummer, G ; Dikic, I |
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| Zeitschrift: | ELife, Jg. 9 (2020-11-13) |
| Veröffentlichung: | Cambridge, UK : eLife Sciences Publications, Ltd., 2012-, 2020 |
| Medientyp: | academicJournal |
| ISSN: | 2050-084X (electronic) |
| DOI: | 10.7554/eLife.58277 |
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