Evidence map›Paper›PMID 15173383›Full record

ArticleNucleic acids research2004

The C-terminal zinc finger of the catalytic subunit of DNA polymerase delta is responsible for direct interaction with the B-subunit.

Javier Sanchez Garcia, Leonora F Ciufo, Xiaowen Yang, Stephen E Kearsey, Stuart A MacNeill

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Trial
  2. Article
  3. Transient ZnProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Human Pol ζ purified with accessory subunits is active in translesion DNA synthesis and complements Pol η in cisplatin bypass.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Review
  15. Article
  16. DNA polymerase delta in DNA replication and genome maintenance.Environmental and molecular mutagenesis · 2012
    Review
  17. Article
  18. Review
  19. Pol31 and Pol32 subunits of yeast DNA polymerase δ are also essential subunits of DNA polymerase ζ.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Subunit sharing among high- and low-fidelity DNA polymerases.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

5 authors at 1 institution in 1 country.

Javier Sanchez GarciaWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.
Leonora F Ciufo
Xiaowen Yang
Stephen E Kearsey
Stuart A MacNeill
Wellcome Centre for Cell Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

DNA polymerase delta (Pol delta) plays a central role in eukaryotic chromosomal DNA replication, repair and recombination. In fission yeast, Pol delta is a tetrameric enzyme, comprising the catalytic subunit Pol3 and three smaller subunits, Cdc1, Cdc27 and Cdm1. Previous studies have demonstrated a direct interaction between Pol3 and Cdc1, the B-subunit of the complex. Here it is shown that removal of the tandem zinc finger modules located at the C-terminus of Pol3 by targeted proteolysis renders the Pol3 protein non-functional in vivo, and that the C-terminal zinc finger module ZnF2 is both necessary and sufficient for binding to the B-subunit in vivo and in vitro. Extensive mutagenesis of the ZnF2 module identifies important residues for B-subunit binding. In particular, disruption of the ZnF2 module by substitution of the putative metal-coordinating cysteines with alanine abolishes B-subunit binding and in vivo function. Finally, evidence is presented suggesting that the ZnF region is post-translationally modified in fission yeast cells.

Indexed as

Zinc FingersAmino Acid SequenceCatalytic DomainCell Cycle ProteinsDNA Polymerase IIIFungal ProteinsMolecular Sequence DataMutationProtein BindingProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesCDC1 protein, S cerevisiaeCell Cycle ProteinsDNA Polymerase IIIFungal ProteinsPOL3 protein, S cerevisiaeProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID15173383
PMCPMC434430
OpenAlexW2156262030

What OpenQuestion holds

Textmetadata
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.