Evidence map›Paper›PMID 26826709›Full record

ArticleNucleic acids research2016

Identification of a conserved 5'-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair.

Ana de Ory, Katja Nagler, Begoña Carrasco, Marina Raguse, Olga Zafra, Ralf Moeller, Miguel de Vega

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

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  6. Frontiers in microbiology · 2021
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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

7 authors at 2 institutions in 2 countries.

Ana de OryCentro de Biología Molecular 'Severo Ochoa' (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, Spain.
Katja NaglerRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, Germany.
Begoña CarrascoCentro Nacional de Biotecnología (Consejo Superior de Investigaciones Científicas), Darwin 3, 28049 Madrid, Spain.
Marina RaguseRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, Germany.
Olga ZafraCentro de Biología Molecular 'Severo Ochoa' (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, Spain.
Ralf MoellerRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, Germany mdevega@cbm.csic.es.
Miguel de VegaCentro de Biología Molecular 'Severo Ochoa' (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, Spain mdevega@cbm.csic.es.ORCID http://orcid.org/0000-0003-1285-7549
Consejo Superior de Investigaciones Científicas · ESDeutsches Zentrum für Luft- und Raumfahrt e. V. (DLR) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacillus subtilis is one of the bacterial members provided with a nonhomologous end joining (NHEJ) system constituted by the DNA-binding Ku homodimer that recruits the ATP-dependent DNA Ligase D (BsuLigD) to the double-stranded DNA breaks (DSBs) ends. BsuLigD has inherent polymerization and ligase activities that allow it to fill the short gaps that can arise after realignment of the broken ends and to seal the resulting nicks, contributing to genome stability during the stationary phase and germination of spores. Here we show that BsuLigD also has an intrinsic 5'-2-deoxyribose-5-phosphate (dRP) lyase activity located at the N-terminal ligase domain that in coordination with the polymerization and ligase activities allows efficient repairing of 2'-deoxyuridine-containing DNA in an in vitro reconstituted Base Excision Repair (BER) reaction. The requirement of a polymerization, a dRP removal and a final sealing step in BER, together with the joint participation of BsuLigD with the spore specific AP endonuclease in conferring spore resistance to ultrahigh vacuum desiccation suggest that BsuLigD could actively participate in this pathway. We demonstrate the presence of the dRP lyase activity also in the homolog protein from the distantly related bacterium Pseudomonas aeruginosa, allowing us to expand our results to other bacterial LigDs.

Indexed as

Bacillus subtilisDNA Breaks, Double-StrandedDNA End-Joining RepairDNA LigasesDNA RepairPhosphorus-Oxygen LyasesPseudomonas aeruginosa5'-deoxyribose phosphate lyaseDNA LigasesPhosphorus-Oxygen Lyases

Identifiers

PMID26826709
PMCPMC4770248
OpenAlexW2279342691

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.