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Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection

MPG-Autoren
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Shin,  Donghyuk
Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biochemistry II Faculty of Medicine, Goethe UniversityFrankfurt, Frankfurt am Main, Germany;
Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany;
Department of Nano-Bioengineering, Incheon National University, Incheon, South Korea;

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Mehdipour,  Ahmad Reza
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Hummer,  Gerhard       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Dikic,  Ivan       
Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biochemistry II Faculty of Medicine, Goethe UniversityFrankfurt, Frankfurt am Main, Germany;
Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Zitation

Shin, D., Bhattacharya, A., Cheng, Y.-L., Alonso, M. C., Mehdipour, A. R., van der Heden van Noort, G. J., et al. (2020). Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection. eLife, 9. doi:10.7554/eLife.58277.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-672B-6
Zusammenfassung
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
egionellaOTU-like deubiquitinases (LOT; 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 Legionella OTU-family shows an extended helical lobe between the Cys-loop and the variable loop, which defines them as a unique class of OTU-deubiquitinases. 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 deubiquitinases and indicate distinct roles in host-pathogen interactions.