Evidence map›Paper›PMID 31704183›Full record

ArticleMolecular cell2020

Tunability of DNA Polymerase Stability during Eukaryotic DNA Replication.

Jacob S Lewis, Lisanne M Spenkelink, Grant D Schauer, Olga Yurieva, Stefan H Mueller, Varsha Natarajan, Gurleen Kaur, Claire Maher, Callum Kay, Michael E O'Donnell and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Genome integrity relies on rapid recycling of DNA Pol III in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Eukaryotic Lagging Strand Synthesis is Distributive.bioRxiv : the preprint server for biology · 2025
    Article
  13. DNA polymerase α-primase can function as a translesion DNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Review
  19. Article
  20. Article

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

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

11 authors at 5 institutions in 2 countries.

Jacob S LewisMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Lisanne M SpenkelinkMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Grant D SchauerDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
Olga YurievaLaboratory of DNA Replication, Rockefeller University, New York, NY 10065, USA; Howard Hughes Medical Institute, Cambridge, MA 02138, USA.
Stefan H MuellerMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Varsha NatarajanMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Gurleen KaurMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Claire MaherMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Callum KayMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia.
Michael E O'DonnellLaboratory of DNA Replication, Rockefeller University, New York, NY 10065, USA; Howard Hughes Medical Institute, Cambridge, MA 02138, USA. Electronic address: odonnel@rockefeller.edu.
Antoine M van OijenMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia; Illawarra Health & Medical Research Institute, Wollongong, NSW 2522, Australia. Electronic address: vanoijen@uow.edu.au.
University of Wollongong · AUIllawarra Health and Medical Research Institute · AUColorado State University · USHoward Hughes Medical Institute · USRockefeller University · US

Funding

Mechanisms of Cell Regulation and TransformationT32CA009673 · NCI · ROCKEFELLER UNIVERSITY · PI KAPOOR, TARUN M. · 1991 to 2018
$7.0M
Biochemical Mechanism and Structure of the Eukaryotic Replication ForkR01GM115809 · NIGMS · ROCKEFELLER UNIVERSITY · PI O'DONNELL, MICHAEL E · 2015 to 2022
$2.6M
BYPASS MECHANISMS IN EUKARYOTIC REPLICATIONR00GM126143 · NIGMS · COLORADO STATE UNIVERSITY · PI SCHAUER, GRANT · 2019 to 2021
$747k
Bypass Mechanisms in Eukaryotic ReplicationK99GM126143 · NIGMS · ROCKEFELLER UNIVERSITY · PI SCHAUER, GRANT · 2018 to 2018
$90k
NCI NIH HHS T32 CA009673NIGMS NIH HHS K99 GM126143NIGMS NIH HHS R00 GM126143NIGMS NIH HHS R01 GM115809
6 · The paper itself

Abstract

Structural and biochemical studies have revealed the basic principles of how the replisome duplicates genomic DNA, but little is known about its dynamics during DNA replication. We reconstitute the 34 proteins needed to form the S. cerevisiae replisome and show how changing local concentrations of the key DNA polymerases tunes the ability of the complex to efficiently recycle these proteins or to dynamically exchange them. Particularly, we demonstrate redundancy of the Pol α-primase DNA polymerase activity in replication and show that Pol α-primase and the lagging-strand Pol δ can be re-used within the replisome to support the synthesis of large numbers of Okazaki fragments. This unexpected malleability of the replisome might allow it to deal with barriers and resource challenges during replication of large genomes.

Indexed as

DNADNA Polymerase IDNA Polymerase IIIDNA PrimaseDNA ReplicationEukaryotic CellsSaccharomyces cerevisiaeDNADNA polymerase alpha-primaseDNA Polymerase IDNA Polymerase IIIDNA PrimaseOkazaki fragmentsDNADNA replicationdynamicsfluorescencemulti-protein complexespolymerasereplication forkreplisomesingle moleculestability

Identifiers

PMID31704183
PMCPMC6943181
OpenAlexW2989260338

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.