Evidence map›Paper›PMID 15175013›Full record

ArticleThe Biochemical journal2004

Purification of Drosophila DNA polymerase zeta by REV1 protein-affinity chromatography.

Ryo Takeuchi, Masahiko Oshige, Makiyo Uchida, Gen Ishikawa, Kei-ichi Takata, Kaori Shimanouchi, Yoshihiro Kanai, Tatsushi Ruike, Hiroshi Morioka, Kengo Sakaguchi

Abstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. REV7 directs DNA repair pathway choice.Trends in cell biology · 2021
    Review
  6. Rescue from replication stress during mitosis.Cell cycle (Georgetown, Tex.) · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Article
  18. Review
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.

Ryo TakeuchiDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda-shi, Chiba-ken 278-8510, Japan.
Masahiko Oshige
Makiyo Uchida
Gen Ishikawa
Kei-ichi Takata
Kaori Shimanouchi
Yoshihiro Kanai
Tatsushi Ruike
Hiroshi Morioka
Kengo Sakaguchi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Studies on the biochemical properties of very-large-size eukaryotic DNA polymerases have been limited by the difficulty in obtaining sufficient purified forms of each enzyme. Our aim was to determine and elucidate the biochemical properties of one such polymerase, pol zeta (DNA polymerase zeta) from Drosophila melanogaster (Dmpol zeta). Using an REV1 (UV-revertible gene 1) protein-affinity column, we have isolated the enzyme directly from Drosophila embryos. Completely purified Dmpol zeta was found to have a molecular mass of approx. 240 kDa, and to be sensitive to aphidicolin and resistant to ddTTP (2',3'-dideoxythymidine-5-triphosphate) and N-ethylmaleimide. The enzyme has a preference for poly(dA)/oligo(dT)(10:1) as a template primer and has high processivity for DNA synthesis. Moreover, Dmpol zeta showed significantly higher fidelity compared with Rattus norvegicus DNA polymerase, an error-prone DNA polymerase, in an M13 forward mutation assay. The activities of bypassing pyrimidine dimers and (6-4) photoproducts and extending from mismatched primer-template termini in (6-4) photoproduct by Dmpol zeta were not detected. Drosophila REV7 interacted with Dmpol zeta in vitro, but did not influence the DNA synthesis activity of Dmpol zeta. The present study is the first report about characterization of purified pol zeta from multicellular organisms, and the second concerning the characterization of yeast pol zeta.

Indexed as

AnimalsBase Pair MismatchChromatography, AffinityDNADNA DamageDNA-Directed DNA PolymeraseDrosophila melanogasterDrosophila ProteinsEmbryo, MammalianEmbryo, NonmammalianMolecular Sequence DataProtein SubunitsRatsDNADNA-Directed DNA PolymeraseDNA polymerase zetaDrosophila ProteinsProtein Subunits

Identifiers

PMID15175013
PMCPMC1133810

What OpenQuestion holds

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Registered trials

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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.