Evidence map›Paper›PMID 32071282›Full record

ArticleLife science alliance2020

The iron-sulfur helicase DDX11 promotes the generation of single-stranded DNA for CHK1 activation.

Anna K Simon, Sandra Kummer, Sebastian Wild, Aleksandra Lezaja, Federico Teloni, Stanislaw K Jozwiakowski, Matthias Altmeyer, Kerstin Gari

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Why cells need iron: a compendium of iron utilisation.Trends in endocrinology and metabolism: TEM · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. DDX11 loss causes replication stress and pharmacologically exploitable DNA repair defects.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Role of the DDX11 DNA Helicase in Warsaw Breakage Syndrome Etiology.International journal of molecular sciences · 2021
    Review
  15. Article
  16. 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 at 1 institution in 1 country.

Anna K SimonInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.
Sandra KummerInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.
Sebastian WildInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.
Aleksandra LezajaDepartment of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
Federico TeloniDepartment of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0953-8010
Stanislaw K JozwiakowskiInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-0553-3530
Matthias AltmeyerDepartment of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
Kerstin GariInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland gari@imcr.uzh.ch.ORCID 0000-0003-1276-8941
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The iron-sulfur (FeS) cluster helicase DDX11 is associated with a human disorder termed Warsaw Breakage Syndrome. Interestingly, one disease-associated mutation affects the highly conserved arginine-263 in the FeS cluster-binding motif. Here, we demonstrate that the FeS cluster in DDX11 is required for DNA binding, ATP hydrolysis, and DNA helicase activity, and that arginine-263 affects FeS cluster binding, most likely because of its positive charge. We further show that DDX11 interacts with the replication factors DNA polymerase delta and WDHD1. In vitro, DDX11 can remove DNA obstacles ahead of Pol δ in an ATPase- and FeS domain-dependent manner, and hence generate single-stranded DNA. Accordingly, depletion of DDX11 causes reduced levels of single-stranded DNA, a reduction of chromatin-bound replication protein A, and impaired CHK1 phosphorylation at serine-345. Taken together, we propose that DDX11 plays a role in dismantling secondary structures during DNA replication, thereby promoting CHK1 activation.

Indexed as

Adenosine TriphosphatasesAnimalsCell Cycle ProteinsCheckpoint Kinase 1DEAD-box RNA HelicasesDNADNA-Binding ProteinsDNA HelicasesDNA Polymerase IIIDNA ReplicationDNA, Single-StrandedHumansReplication Protein ASf9 CellsAdenosine TriphosphatasesCell Cycle ProteinsCheckpoint Kinase 1CHEK1 protein, humanDDX11 protein, humanDEAD-box RNA HelicasesDNADNA-Binding ProteinsDNA HelicasesDNA Polymerase IIIDNA, Single-StrandedReplication Protein ARPA1 protein, humanWDHD1 protein, human

Identifiers

PMID32071282
PMCPMC7032568
OpenAlexW3007587490

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.