Evidence map›Paper›PMID 22434886›Full record

ArticleNucleic acids research2012

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

Maria Manosas, Michelle M Spiering, Fangyuan Ding, Vincent Croquette, Stephen J Benkovic

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Mechanism of eukaryotic origin unwinding is a dual helicase DNA shearing process.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. The nucleotide addition cycle of the SARS-CoV-2 polymerase.bioRxiv : the preprint server for biology · 2021
    Article
  16. Article
  17. DNA replication:Computational and structural biotechnology journal · 2021
    Review
  18. DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021
    Review
  19. Review
  20. 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.

Maria ManosasDépartement de Physique, Laboratoire de Physique Statistique, Ecole Normale Supérieure, Université Pierre et Marie Curie Université Paris 06, Université Paris Diderot, Centre National de la Recherche Scientifique, Paris 75005, France.
Michelle M Spiering
Fangyuan Ding
Vincent Croquette
Stephen J Benkovic

Funding

PHOSPHATE ACTIVATION MECHANISMSR01GM013306 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BENKOVIC, STEPHEN J · 1985 to 2022
$10.0M
NIGMS NIH HHS GM013306NIGMS NIH HHS R01 GM013306
6 · The paper itself

Abstract

Rapid and processive leading-strand DNA synthesis in the bacteriophage T4 system requires functional coupling between the helicase and the holoenzyme, consisting of the polymerase and trimeric clamp loaded by the clamp loader. We investigated the mechanism of this coupling on a DNA hairpin substrate manipulated by a magnetic trap. In stark contrast to the isolated enzymes, the coupled system synthesized DNA at the maximum rate without exhibiting fork regression or pauses. DNA synthesis and unwinding activities were coupled at low forces, but became uncoupled displaying separate activities at high forces or low dNTP concentration. We propose a collaborative model in which the helicase releases the fork regression pressure on the holoenzyme allowing it to adopt a processive polymerization conformation and the holoenzyme destabilizes the first few base pairs of the fork thereby increasing the efficiency of helicase unwinding. The model implies that both enzymes are localized at the fork, but does not require a specific interaction between them. The model quantitatively reproduces homologous and heterologous coupling results under various experimental conditions.

Indexed as

Bacillus PhagesBacteriophage T4DNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA ReplicationExodeoxyribonucleasesHoloenzymesMultienzyme ComplexesReplisomesViral Proteinsbacteriophage T7 induced DNA polymeraseDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesExodeoxyribonucleasesgene 41 protein, Enterobacteria phage T4gene 43 protein, Enterobacteria phage T4gp32 protein, Enterobacteria phage T4HoloenzymesMultienzyme ComplexesReplisomesViral Proteins

Identifiers

PMID22434886
PMCPMC3401439

What OpenQuestion holds

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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.