Evidence map›Paper›PMID 21859751›Full record

ArticleNucleic acids research2011

Polynucleotide phosphorylase exonuclease and polymerase activities on single-stranded DNA ends are modulated by RecN, SsbA and RecA proteins.

Paula P Cardenas, Thomas Carzaniga, Sandro Zangrossi, Federica Briani, Esther Garcia-Tirado, Gianni Dehò, Juan C Alonso

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Structural insights into RNA recognition by theProceedings of the National Academy of Sciences of the United States of America · 2026
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  6. Exoribonuclease RNase R protects AntarcticApplied and environmental microbiology · 2023
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  10. Mini review: Enzyme-based DNA synthesis and selective retrieval for data storage.Computational and structural biotechnology journal · 2021
    Review
  11. Article
  12. Frontiers in microbiology · 2019
    Article
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  15. Article
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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.

Paula P CardenasCentro Nacional de Biotecnología-CSIC, Darwin 3, 28049 Madrid, Spain.
Thomas Carzaniga
Sandro Zangrossi
Federica Briani
Esther Garcia-Tirado
Gianni Dehò
Juan C Alonso
University of Milan · ITCentro Nacional de Biotecnología · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacillus subtilis pnpA gene product, polynucleotide phosphorylase (PNPase), is involved in double-strand break (DSB) repair via homologous recombination (HR) or non-homologous end-joining (NHEJ). RecN is among the first responders to localize at the DNA DSBs, with PNPase facilitating the formation of a discrete RecN focus per nucleoid. PNPase, which co-purifies with RecA and RecN, was able to degrade single-stranded (ss) DNA with a 3' → 5' polarity in the presence of Mn(2+) and low inorganic phosphate (Pi) concentration, or to extend a 3'-OH end in the presence dNDP · Mn(2+). Both PNPase activities were observed in evolutionarily distant bacteria (B. subtilis and Escherichia coli), suggesting conserved functions. The activity of PNPase was directed toward ssDNA degradation or polymerization by manipulating the Pi/dNDPs concentrations or the availability of RecA or RecN. In its dATP-bound form, RecN stimulates PNPase-mediated polymerization. ssDNA phosphorolysis catalyzed by PNPase is stimulated by RecA, but inhibited by SsbA. Our findings suggest that (i) the PNPase degradative and polymerizing activities might play a critical role in the transition from DSB sensing to end resection via HR and (ii) by blunting a 3'-tailed duplex DNA, in the absence of HR, B. subtilis PNPase might also contribute to repair via NHEJ.

Indexed as

Bacillus subtilisBacterial ProteinsDeoxyadenine NucleotidesDNA-Directed DNA PolymeraseDNA Restriction EnzymesDNA, Single-StrandedEscherichia coliExodeoxyribonucleasesManganesePolyribonucleotide NucleotidyltransferaseRec A Recombinases2'-deoxyadenosine triphosphateBacterial ProteinsDeoxyadenine NucleotidesDNA-Directed DNA PolymeraseDNA Restriction EnzymesDNA, Single-StrandedExodeoxyribonucleasesManganesePolyribonucleotide NucleotidyltransferaseRec A RecombinasesRecN protein, Bacteria

Identifiers

PMID21859751
PMCPMC3241651
OpenAlexW2152515534

What OpenQuestion holds

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LicenceCC BY-NC
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.