Evidence map›Paper›PMID 22119860›Full record

ArticleNature chemical biology2011

Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes.

Daili J A Netz, Carrie M Stith, Martin Stümpfig, Gabriele Köpf, Daniel Vogel, Heide M Genau, Joseph L Stodola, Roland Lill, Peter M J Burgers, Antonio J Pierik

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 236 papers.

0numbers the graph read from it
0cells of the map it votes in
236citing papers in PubMed
10.1field-weighted citation impact, top 1% 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

236 citing papers in PubMed, 387 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Eukaryotic Lagging Strand Synthesis is Distributive.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

176 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Daili J A NetzInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Marburg, Germany.
Carrie M Stith
Martin Stümpfig
Gabriele Köpf
Daniel Vogel
Heide M Genau
Joseph L Stodola
Roland Lill
Peter M J Burgers
Antonio J Pierik
Philipps University of Marburg · DEWashington University in St. Louis · US

Funding

ENZYMOLOGY OF REPLICATION OF YEAST CHROMOSOMAL DNAR01GM032431 · NIGMS · WASHINGTON UNIVERSITY · PI BURGERS, PETER M · 1985 to 2015
$6.5M
NIGMS NIH HHS GM032431NIGMS NIH HHS R01 GM032431
6 · The paper itself

Abstract

The eukaryotic replicative DNA polymerases (Pol α, δ and ɛ) and the major DNA mutagenesis enzyme Pol ζ contain two conserved cysteine-rich metal-binding motifs (CysA and CysB) in the C-terminal domain (CTD) of their catalytic subunits. Here we demonstrate by in vivo and in vitro approaches the presence of an essential [4Fe-4S] cluster in the CysB motif of all four yeast B-family DNA polymerases. Loss of the [4Fe-4S] cofactor by cysteine ligand mutagenesis in Pol3 destabilized the CTD and abrogated interaction with the Pol31 and Pol32 subunits. Reciprocally, overexpression of accessory subunits increased the amount of the CTD-bound Fe-S cluster. This implies an important physiological role of the Fe-S cluster in polymerase complex stabilization. Further, we demonstrate that the Zn-binding CysA motif is required for PCNA-mediated Pol δ processivity. Together, our findings show that the function of eukaryotic replicative DNA polymerases crucially depends on different metallocenters for accessory subunit recruitment and replisome stability.

Indexed as

Catalytic DomainDNA-Directed DNA PolymeraseIronModels, MolecularProtein BindingProtein Structure, QuaternarySaccharomyces cerevisiaeSulfurDNA-Directed DNA PolymeraseIronSulfur

Identifiers

PMID22119860
PMCPMC3241888
OpenAlexW2120269671

What OpenQuestion holds

Textmetadata
LicenceTDM
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.