Evidence map›Paper›PMID 39377462›Full record

ArticleeLife2024

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids.

Emily L Dearlove, Chatrin Chatrin, Lori Buetow, Syed F Ahmed, Tobias Schmidt, Martin Bushell, Brian O Smith, Danny T Huang

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Review
  2. Article
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  6. Review
  7. Review
  8. Article
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  10. Article
  11. Article
  12. Article
  13. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
  14. Insights into non-proteinaceous ubiquitination.Biochemical Society transactions · 2025
    Review
  15. Review
  16. Article
  17. Review
  18. Review
  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

8 authors.

Emily L Dearlove *Cancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.
Chatrin Chatrin *Cancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.
Lori BuetowCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.
Syed F AhmedCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.ORCID https://orcid.org/0000-0003-1033-2538
Tobias SchmidtCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.
Martin BushellCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.
Brian O SmithSchool of Molecular Biosciences, University of Glasgow, Glasgow, United Kingdom.
Danny T HuangCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow, United Kingdom.ORCID https://orcid.org/0000-0002-6192-259X

Funding

Cancer Research UK 24388Cancer Research UK 29252Cancer Research UK 30062Cancer Research UK A29252Cancer Research UK A29256Cancer Research UK DRCQQR-JUN24/100002Cancer Research UK Scotland Institute A31287Cancer Research UK Scotland Institute C596/A17196
6 · The paper itself

Abstract

Ubiquitination typically involves covalent linking of ubiquitin (Ub) to a lysine residue on a protein substrate. Recently, new facets of this process have emerged, including Ub modification of non-proteinaceous substrates like ADP-ribose by the DELTEX E3 ligase family. Here, we show that the DELTEX family member DTX3L expands this non-proteinaceous substrate repertoire to include single-stranded DNA and RNA. Although the N-terminal region of DTX3L contains single-stranded nucleic acid binding domains and motifs, the minimal catalytically competent fragment comprises the C-terminal RING and DTC domains (RD). DTX3L-RD catalyses ubiquitination of the 3'-end of single-stranded DNA and RNA, as well as double-stranded DNA with a 3' overhang of two or more nucleotides. This modification is reversibly cleaved by deubiquitinases. NMR and biochemical analyses reveal that the DTC domain binds single-stranded DNA and facilitates the catalysis of Ub transfer from RING-bound E2-conjugated Ub. Our study unveils the direct ubiquitination of nucleic acids by DTX3L, laying the groundwork for understanding its functional implications.

Indexed as

DNA, Single-StrandedUbiquitinationUbiquitin-Protein LigasesHumansProtein BindingRNAUbiquitinDNA, Single-StrandedRNAUbiquitinUbiquitin-Protein Ligasesbiochemistrychemical biologyDTX3Lhumannucleic aicdsubiquitinubiquitin ligase

Identifiers

PMID39377462
PMCPMC11460948

What OpenQuestion holds

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Registered trials

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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.