Evidence map›Paper›PMID 24957605›Full record

ArticleNucleic acids research2014

DNA polymerase IV mediates efficient and quick recovery of replication forks stalled at N2-dG adducts.

Mio Ikeda, Asako Furukohri, Gaelle Philippin, Edward Loechler, Masahiro Tatsumi Akiyama, Tsutomu Katayama, Robert P Fuchs, Hisaji Maki

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  3. Article
  4. Article
  5. Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Review
  8. The methylation-independent mismatch repair machinery inMicrobiology (Reading, England) · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

8 authors.

Mio IkedaDivision of Integrated Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Asako FurukohriDivision of Integrated Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan furukori@bs.naist.jp.
Gaelle PhilippinCRCM, CNRS, UMR7258; Inserm, U1068; Institut Paoli-Calmettes; Aix-Marseille Universite, UM105, F13009 Marseille, France.
Edward LoechlerBiology Department, Boston University, Boston, MA 02215, USA.
Masahiro Tatsumi AkiyamaDivision of Integrated Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Tsutomu KatayamaDepartment of Molecular Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Robert P FuchsCRCM, CNRS, UMR7258; Inserm, U1068; Institut Paoli-Calmettes; Aix-Marseille Universite, UM105, F13009 Marseille, France furukori@bs.naist.jp.
Hisaji MakiDivision of Integrated Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan furukori@bs.naist.jp.

Funding

MUTAGENIC CONSEQUENCES OF BENZO[A]PYRENE ADDUCTSR01ES003775 · NIEHS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LOECHLER, EDWARD L · 1985 to 2011
$3.7M
NIEHS NIH HHS R01ES003775
6 · The paper itself

Abstract

Escherichia coli DNA polymerase IV (Pol IV, also known as DinB) is a Y-family DNA polymerase capable of catalyzing translesion DNA synthesis (TLS) on certain DNA lesions, and accumulating data suggest that Pol IV may play an important role in copying various kinds of spontaneous DNA damage including N(2)-dG adducts and alkylated bases. Pol IV has a unique ability to coexist with Pol III on the same β clamp and to positively dissociate Pol III from β clamp in a concentration-dependent manner. Reconstituting the entire process of TLS in vitro using E. coli replication machinery and Pol IV, we observed that a replication fork stalled at (-)-trans-anti-benzo[a]pyrene-N(2)-dG lesion on the leading strand was efficiently and quickly recovered via two sequential switches from Pol III to Pol IV and back to Pol III. Our results suggest that TLS by Pol IV smoothes the way for the replication fork with minimal interruption.

Indexed as

BenzopyrenesDNA AdductsDNA ReplicationDeoxyguanosineDNADNA Polymerase betaDNA Polymerase IIIEscherichia coliEscherichia coli Proteinsbenzo(a)pyrene N2-dG adductBenzopyrenesDeoxyguanosineDinB protein, E coliDNADNA AdductsDNA Polymerase betaDNA Polymerase IIIEscherichia coli Proteins

Identifiers

PMID24957605
PMCPMC4117773

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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.