Evidence map›Paper›PMID 19305001›Full record

ArticleNucleic acids research2009

XRCC1 interacts with the p58 subunit of DNA Pol alpha-primase and may coordinate DNA repair and replication during S phase.

Nicolas Lévy, Maren Oehlmann, François Delalande, Heinz Peter Nasheuer, Alain Van Dorsselaer, Valérie Schreiber, Gilbert de Murcia, Josiane Ménissier-de Murcia, Domenico Maiorano, Anne Bresson

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Base excision repair and cancer.Cancer letters · 2012
    Review
  8. Article
  9. Structural studies of the PARP-1 BRCT domain.BMC structural biology · 2011
    Article
  10. Article
  11. 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

10 authors at 6 institutions in 2 countries.

Nicolas LévyFRE 3211, Institut de Recherche de l'Ecole de Biotechnologie de Strasbourg, CNRS/Université de Strasbourg, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard S. Brant, BP 10413, F-67412, Illkirch Cedex, France.
Maren Oehlmann
François Delalande
Heinz Peter Nasheuer
Alain Van Dorsselaer
Valérie Schreiber
Gilbert de Murcia
Josiane Ménissier-de Murcia
Domenico Maiorano
Anne Bresson
Biotechnologie et Signalisation Cellulaire · FRCentre National de la Recherche Scientifique · FRUniversité de Strasbourg · FRInstitut de Chimie de Strasbourg · FRInstitut de génétique et de biologie moléculaire et cellulaire · FROllscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Repair of single-stranded DNA breaks before DNA replication is critical in maintaining genomic stability; however, how cells deal with these lesions during S phase is not clear. Using combined approaches of proteomics and in vitro and in vivo protein-protein interaction, we identified the p58 subunit of DNA Pol alpha-primase as a new binding partner of XRCC1, a key protein of the single strand break repair (SSBR) complex. In vitro experiments reveal that the binding of poly(ADP-ribose) to p58 inhibits primase activity by competition with its DNA binding property. Overexpression of the XRCC1-BRCT1 domain in HeLa cells induces poly(ADP-ribose) synthesis, PARP-1 and XRCC1-BRCT1 poly(ADP-ribosyl)ation and a strong S phase delay in the presence of DNA damage. Addition of recombinant XRCC1-BRCT1 to Xenopus egg extracts slows down DNA synthesis and inhibits the binding of PCNA, but not MCM2 to alkylated chromatin, thus indicating interference with the assembly of functional replication forks. Altogether these results suggest a critical role for XRCC1 in connecting the SSBR machinery with the replication fork to halt DNA synthesis in response to DNA damage.

Indexed as

DNA RepairDNA ReplicationAnimalsChromatinDNADNA-Binding ProteinsDNA DamageDNA Polymerase IDNA PrimaseHeLa CellsHumansPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein Interaction Domains and MotifsS PhaseXenopus laevisChromatinDNADNA-Binding ProteinsDNA polymerase alpha-primaseDNA Polymerase IDNA PrimasePARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesPRIM2 protein, humanX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID19305001
PMCPMC2691816
OpenAlexW2164185800

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.