Evidence map›Paper›PMID 32567101›Full record

ArticleThe EMBO journal2020

Identification and characterization of diverse OTU deubiquitinases in bacteria.

Alexander F Schubert, Justine V Nguyen, Tyler G Franklin, Paul P Geurink, Cameron G Roberts, Daniel J Sanderson, Lauren N Miller, Huib Ovaa, Kay Hofmann, Jonathan N Pruneda and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  4. A diverse family of bacterial deubiquitinases is defined by theProceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 5 countries.

Alexander F Schubert *Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-1834-3787
Justine V Nguyen *Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.ORCID 0000-0001-9739-5261
Tyler G FranklinDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.ORCID 0000-0002-0311-1190
Paul P GeurinkOncode Institute & Department of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, The Netherlands.ORCID 0000-0003-1849-1111
Cameron G RobertsDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.ORCID 0000-0002-0115-7013
Daniel J SandersonDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.ORCID 0000-0002-0516-814X
Lauren N MillerDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.ORCID 0000-0001-6982-5041
Huib OvaaOncode Institute & Department of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, The Netherlands.ORCID 0000-0002-0068-054X
Kay HofmannInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID 0000-0002-2289-9083
Jonathan N PrunedaMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-0304-4418
David KomanderMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-8092-4320
Oregon Health & Science University · USLeiden University · NLMRC Laboratory of Molecular Biology · GBThe University of Melbourne · AUUniversity of Cologne · DE

Funding

Program in Molecular and Cellular BiosciencesT32GM071338 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MASLEN, CHERYL L · 2005 to 2020
$3.5M
European Research Council 309756European Research Council 724804Medical Research Council MC_U105192732Medical Research Council U105192732NIGMS NIH HHS T32 GM071338
6 · The paper itself

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.

Indexed as

Bacterial ProteinsDeubiquitinating EnzymesProtein FoldingLegionellaPolyubiquitinSubstrate SpecificityBacterial ProteinsDeubiquitinating EnzymesPolyubiquitinbacterial effectordeubiquitinasepathogenprotein structureubiquitin

Identifiers

PMID32567101
PMCPMC7396840
OpenAlexW3035797211

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.