Evidence map›Paper›PMID 19433509›Full record

ArticleNucleic acids research2009

Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair.

Paula P Cardenas, Begoña Carrasco, Humberto Sanchez, Gintaras Deikus, David H Bechhofer, Juan C Alonso

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2025
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  4. Review
  5. Review
  6. Article
  7. Exoribonuclease RNase R protects AntarcticApplied and environmental microbiology · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Frontiers in microbiology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Blueprint of a Minimal Cell: MiniBacillus.Microbiology and molecular biology reviews : MMBR · 2016
    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

6 authors at 2 institutions in 2 countries.

Paula P CardenasDepartment of Microbial Biotechnology, Centro Nacional de Biotecnología, CSIC, C/Darwin 3, Campus Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Begoña Carrasco
Humberto Sanchez
Gintaras Deikus
David H Bechhofer
Juan C Alonso
Icahn School of Medicine at Mount Sinai · USCentro Nacional de Biotecnología · ES

Funding

INITIATION OF MRNA DECAY IN BACILLUS SUBTILISR01GM048804 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI BECHHOFER, DAVID H · 1993 to 2010
$2.9M
NIGMS NIH HHS GM48804
6 · The paper itself

Abstract

In the presence of Mn(2+), an activity in a preparation of purified Bacillus subtilis RecN degrades single-stranded (ss) DNA with a 3' --> 5' polarity. This activity is not associated with RecN itself, because RecN purified from cells lacking polynucleotide phosphorylase (PNPase) does not show the exonuclease activity. We show here that, in the presence of Mn(2+) and low-level inorganic phosphate (P(i)), PNPase degrades ssDNA. The limited end-processing of DNA is regulated by ATP and is inactive in the presence of Mg(2+) or high-level P(i). In contrast, the RNase activity of PNPase requires Mg(2+) and P(i), suggesting that PNPase degradation of RNA and ssDNA occur by mutually exclusive mechanisms. A null pnpA mutation (DeltapnpA) is not epistatic with Delta recA, but is epistatic with DeltarecN and Delta ku, which by themselves are non-epistatic. The addA5, Delta recO, Delta recQ (Delta recJ), Delta recU and Delta recG mutations (representative of different epistatic groups), in the context of DeltapnpA, demonstrate gain- or loss-of-function by inactivation of repair-by-recombination, depending on acute or chronic exposure to the damaging agent and the nature of the DNA lesion. Our data suggest that PNPase is involved in various nucleic acid metabolic pathways, and its limited ssDNA exonuclease activity plays an important role in RecA-dependent and RecA-independent repair pathways.

Indexed as

DNA RepairBacillus subtilisBacterial ProteinsCations, DivalentDNA Restriction EnzymesDNA, Single-StrandedEpigenesis, GeneticExodeoxyribonucleasesExoribonucleasesManganeseMutationPolyribonucleotide NucleotidyltransferaseBacterial ProteinsCations, DivalentDNA Restriction EnzymesDNA, Single-StrandedExodeoxyribonucleasesExoribonucleasesManganesePolyribonucleotide NucleotidyltransferaseRecN protein, Bacteria

Identifiers

PMID19433509
PMCPMC2709576
OpenAlexW1966287132

What OpenQuestion holds

Textmetadata
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.