Evidence map›Paper›PMID 32393759›Full record

ArticleNature communications2020

A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi.

Jason M Berk, Christopher Lim, Judith A Ronau, Apala Chaudhuri, Hongli Chen, John F Beckmann, J Patrick Loria, Yong Xiong, Mark Hochstrasser

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Transformation and allelic exchange inbioRxiv : the preprint server for biology · 2026
    Article
  3. A diverse family of bacterial deubiquitinases is defined by theProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Cocrystallization of ubiquitin-deubiquitinase complexes through disulfide linkage.Acta crystallographica. Section D, Structural biology · 2023
    Article
  11. Review
  12. TheProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors at 2 institutions in 1 country.

Jason M Berk *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Christopher Lim *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Judith A RonauDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Apala ChaudhuriDepartment of Chemistry, Yale University, New Haven, CT, 06520, USA.
Hongli ChenDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
John F BeckmannDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
J Patrick LoriaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Yong XiongDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA. yong.xiong@yale.edu.ORCID http://orcid.org/0000-0001-9625-9313
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA. mark.hochstrasser@yale.edu.ORCID http://orcid.org/0000-0002-1131-5484
Yale University · USAbbVie (United States) · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Mechanisms of Cell Regulation and Manipulation by the Ubiquitin SystemR35GM136325 · NIGMS · YALE UNIVERSITY · PI Mark W Hochstrasser · 2020 to 2026
$6.5M
FUNCTIONS AND MECHANISMS OF DEUBIQUITINATING ENZYMESR01GM053756 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1996 to 2019
$6.5M
DEGRADTION OF SHORT-LIVED REGULATORY PROTEINS IN YEASTR01GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1992 to 2020
$3.6M
Multifaceted interactions between lentiviral Vif and host molecules for viral infectivity enhancementR37AI116313 · NIAID · YALE UNIVERSITY · PI Yong Xiong · 2021 to 2026
$3.2M
Computational and Biochemical Studies of Temperature Effects on Allostery in the Imidazole Glycerol Phosphate Synthase (IGPS) from T. maritimaR01GM106121 · NIGMS · YALE UNIVERSITY · PI BATISTA, VICTOR S, LORIA, JOSEPH P · 2014 to 2021
$2.3M
Recognition of Viral DNA by APOBEC3 Proteins and their Antagonization by HIV VifR01AI116313 · NIAID · YALE UNIVERSITY · PI XIONG, YONG · 2015 to 2019
$2.1M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Investigation of the Broad Substrate Specificity of an ER Membrane Ubiquitin LigaseF32GM113456 · NIGMS · YALE UNIVERSITY · PI BERK, JASON MICHAEL · 2015 to 2016
$112k
NCRR NIH HHS S10 RR029205NIAID NIH HHS R01 AI116313NIAID NIH HHS R37 AI116313NIGMS NIH HHS F32 GM113456NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM046904NIGMS NIH HHS R01 GM053756NIGMS NIH HHS R01 GM106121NIGMS NIH HHS R35 GM136325NIGMS NIH HHS T32 GM008283
6 · The paper itself

Abstract

Ubiquitin mediated signaling contributes critically to host cell defenses during pathogen infection. Many pathogens manipulate the ubiquitin system to evade these defenses. Here we characterize a likely effector protein bearing a deubiquitylase (DUB) domain from the obligate intracellular bacterium Orientia tsutsugamushi, the causative agent of scrub typhus. The Ulp1-like DUB prefers ubiquitin substrates over ubiquitin-like proteins and efficiently cleaves polyubiquitin chains of three or more ubiquitins. The co-crystal structure of the DUB (OtDUB) domain with ubiquitin revealed three bound ubiquitins: one engages the S1 site, the second binds an S2 site contributing to chain specificity and the third binds a unique ubiquitin-binding domain (UBD). The UBD modulates OtDUB activity, undergoes a pronounced structural transition upon binding ubiquitin, and binds monoubiquitin with an unprecedented ~5 nM dissociation constant. The characterization and high-resolution structure determination of this enzyme should aid in its development as a drug target to counter Orientia infections.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayHydrophobic and Hydrophilic InteractionsLysineOrientia tsutsugamushiProtein BindingProtein DomainsScrub TyphusSubstrate SpecificityThermodynamicsUbiquitinsBacterial ProteinsLysineUbiquitins

Identifiers

PMID32393759
PMCPMC7214410
OpenAlexW3023472230

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.