Evidence map›Paper›PMID 32023456›Full record

ArticleCell reports2020

DNA ADP-Ribosylation Stalls Replication and Is Reversed by RecF-Mediated Homologous Recombination and Nucleotide Excision Repair.

Emeline Lawarée, Gytis Jankevicius, Charles Cooper, Ivan Ahel, Stephan Uphoff, Christoph M Tang

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.9field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023
    Review
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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

6 authors at 1 institution in 1 country.

Emeline LawaréeSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Gytis JankeviciusSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Charles CooperSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Stephan UphoffDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Christoph M TangSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK. Electronic address: christoph.tang@path.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 102908/Z/13/ZWellcome Trust 206159/Z/17/Z
6 · The paper itself

Abstract

ADP-ribosylation of proteins is crucial for fundamental cellular processes. Despite increasing examples of DNA ADP-ribosylation, the impact of this modification on DNA metabolism and cell physiology is unknown. Here, we show that the DarTG toxin-antitoxin system from enteropathogenic Escherichia coli (EPEC) catalyzes reversible ADP-ribosylation of single-stranded DNA (ssDNA). The DarT toxin recognizes specific sequence motifs. EPEC DarG abrogates DarT toxicity by two distinct mechanisms: removal of DNA ADP-ribose (ADPr) groups and DarT sequestration. Furthermore, we investigate how cells recognize and deal with DNA ADP-ribosylation. We demonstrate that DNA ADPr stalls replication and is perceived as DNA damage. Removal of ADPr from DNA requires the sequential activity of two DNA repair pathways, with RecF-mediated homologous recombination likely to transfer ADP-ribosylation from single- to double-stranded DNA (dsDNA) and subsequent nucleotide excision repair eliminating the lesion. Our work demonstrates that these DNA repair pathways prevent the genotoxic effects of DNA ADP-ribosylation.

Indexed as

ADP-RibosylationDNA RepairDNA ReplicationHomologous RecombinationAdenosine Diphosphate RiboseDNA, BacterialDNA-Binding ProteinsEnteropathogenic Escherichia coliEscherichia coli ProteinsMicrobial ViabilityModels, BiologicalSOS Response, GeneticsAdenosine Diphosphate RiboseDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsrecF protein, E coliDNA ADP-ribosylationDNA damageEPECnucleotide excision repairSOS responsetoxin-antitoxin system

Identifiers

PMID32023456
PMCPMC7003065
OpenAlexW3005150305

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.