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  Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection

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.

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 Creators:
Shin, Donghyuk1, 2, 3, 4, Author              
Bhattacharya, Anshu2, 3, Author
Cheng, Yi-Lin2, 3, Author
Alonso, Marta Campos3, Author
Mehdipour, Ahmad Reza5, Author              
van der Heden van Noort, Gerbrand J.6, Author
Ovaa, Huib6, Author
Hummer, Gerhard5, 7, Author              
Dikic, Ivan1, 2, 3, Author              
Affiliations:
1Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society, ou_3004983              
2Institute of Biochemistry II Faculty of Medicine, Goethe UniversityFrankfurt, Frankfurt am Main, Germany, ou_persistent22              
3Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
4Department of Nano-Bioengineering, Incheon National University, Incheon, South Korea, ou_persistent22              
5Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
6Oncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, The Netherlands, ou_persistent22              
7Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: biochemistry, chemical biology, human
 Abstract: 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.

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Language(s): eng - English
 Dates: 2020-11-13
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.58277
BibTex Citekey: shin_bacterial_2020
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 9 Sequence Number: - Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X