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Identification and characterization of diverse OTU deubiquitinases in bacteria

DOI: 10.15252/embj.2020105127 DOI Help

Authors: Alexander F. Schubert (Medical Research Council Laboratory of Molecular Biology) , Justine V Nguyen (Oregon Health & Science University) , Tyler G. Franklin (Oregon Health & Science University,) , Paul P. Geurink (Leiden University Medical Centre) , Cameron G. Roberts (Oregon Health & Science University) , Daniel J. Sanderson (Oregon Health & Science University) , Lauren N. Miller (Oregon Health & Science University) , Huib Ovaa (Leiden University Medical Centre) , Kay Hofmann (University of Cologne) , Jonathan N. Pruneda (Medical Research Council Laboratory of Molecular Biology; Oregon Health & Science University) , David Komander (Medical Research Council Laboratory of Molecular Biology; The Walter and Eliza Hall Institute of Medical Research; The University of Melbourne)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Embo Journal , VOL 81

State: Published (Approved)
Published: June 2020
Diamond Proposal Number(s): 8547 , 11235

Open Access Open Access

Abstract: Manipulation of host ubiquitin signaling is becoming an increasingly apparent evolutionary strategy among bacterial and viral pathogens. By removing host ubiquitin signals, for example, invading pathogens can inactivate immune response pathways and evade detection. The ovarian tumor (OTU) family of deubiquitinases regulates diverse ubiquitin signals in humans. Viral pathogens have also extensively co‐opted the OTU fold to subvert host signaling, but the extent to which bacteria utilize the OTU fold was unknown. We have predicted and validated a set of OTU deubiquitinases encoded by several classes of pathogenic bacteria. Biochemical assays highlight the ubiquitin and polyubiquitin linkage specificities of these bacterial deubiquitinases. By determining the ubiquitin‐bound structures of two examples, we demonstrate the novel strategies that have evolved to both thread an OTU fold and recognize a ubiquitin substrate. With these new examples, we perform the first cross‐kingdom structural analysis of the OTU fold that highlights commonalities among distantly related OTU deubiquitinases.

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 01/07/2020 09:08

Documents:
embj.2020105127.pdf

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Infectious Diseases Pathogens Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)