Evidence map›Paper›PMID 22434889›Full record

ArticleNucleic acids research2012

Mechanism of strand displacement synthesis by DNA replicative polymerases.

Maria Manosas, Michelle M Spiering, Fangyuan Ding, David Bensimon, Jean-François Allemand, Stephen J Benkovic, Vincent Croquette

Open access · goldAbstract 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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 74 citations in OpenAlex.

  1. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. Review
  3. DNA Polymerase Locks Replication Fork Under Stress.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Bst polymerase - a humble relative of Taq polymerase.Computational and structural biotechnology journal · 2023
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. The nucleotide addition cycle of the SARS-CoV-2 polymerase.bioRxiv : the preprint server for biology · 2021
    Article
  17. Article
  18. Review
  19. DNA replication:Computational and structural biotechnology journal · 2021
    Review
  20. DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021
    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

7 authors at 1 institution in 3 countries.

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
David Bensimon
Jean-François Allemand
Stephen J Benkovic
Vincent Croquette
Centre National de la Recherche Scientifique · FR

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

Replicative holoenzymes exhibit rapid and processive primer extension DNA synthesis, but inefficient strand displacement DNA synthesis. We investigated the bacteriophage T4 and T7 holoenzymes primer extension activity and strand displacement activity on a DNA hairpin substrate manipulated by a magnetic trap. Holoenzyme primer extension activity is moderately hindered by the applied force. In contrast, the strand displacement activity is strongly stimulated by the applied force; DNA polymerization is favoured at high force, while a processive exonuclease activity is triggered at low force. We propose that the DNA fork upstream of the holoenzyme generates a regression pressure which inhibits the polymerization-driven forward motion of the holoenzyme. The inhibition is generated by the distortion of the template strand within the polymerization active site thereby shifting the equilibrium to a DNA-protein exonuclease conformation. We conclude that stalling of the holoenzyme induced by the fork regression pressure is the basis for the inefficient strand displacement synthesis characteristic of replicative polymerases. The resulting processive exonuclease activity may be relevant in replisome disassembly to reset a stalled replication fork to a symmetrical situation. Our findings offer interesting applications for single-molecule DNA sequencing.

Indexed as

DNADNA-Directed DNA PolymeraseDNA ReplicationHoloenzymesKineticsSequence Analysis, DNAViral Proteinsbacteriophage T7 induced DNA polymeraseDNADNA-Directed DNA Polymerasegene 43 protein, Enterobacteria phage T4HoloenzymesViral Proteins

Identifiers

PMID22434889
PMCPMC3401438
OpenAlexW2006294065

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.