Evidence map›Paper›PMID 24630996›Full record

ArticleCell reports2014

Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps.

Manjula Pandey, Smita S Patel

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

  1. Structural Activation of DNA Unwinding by MCM8/9/HROB.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024
    Review
  7. DNA Polymerase Locks Replication Fork Under Stress.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. 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
  10. Article
  11. Article
  12. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
    Review
  13. Article
  14. Review
  15. DNA replication:Computational and structural biotechnology journal · 2021
    Review
  16. Review
  17. DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021
    Review
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

Manjula PandeyDepartment of Biochemistry and Molecular Biology, Rutgers, The State University of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
Smita S PatelDepartment of Biochemistry and Molecular Biology, Rutgers, The State University of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA. Electronic address: patelss@rwjms.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

MECHANISTIC STUDIES OF HEXAMERIC HELICASESR01GM055310 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PATEL, SMITA S · 1997 to 2015
$4.6M
Mechanism and Regulation of Transcription InitiationR37GM051966 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PATEL, SMITA S · 2007 to 2015
$3.8M
NIGMS NIH HHS GM55310NIGMS NIH HHS R01 GM055310NIGMS NIH HHS R37 GM051966
6 · The paper itself

Abstract

By simultaneously measuring DNA synthesis and dNTP hydrolysis, we show that T7 DNA polymerase and T7 gp4 helicase move in sync during leading-strand synthesis, taking one-nucleotide steps and hydrolyzing one dNTP per base-pair unwound/copied. The cooperative catalysis enables the helicase and polymerase to move at a uniformly fast rate without guanine:cytosine (GC) dependency or idling with futile NTP hydrolysis. We show that the helicase and polymerase are located close to the replication fork junction. This architecture enables the polymerase to use its strand-displacement synthesis to increase the unwinding rate, whereas the helicase aids this process by translocating along single-stranded DNA and trapping the unwound bases. Thus, in contrast to the helicase-only unwinding model, our results suggest a model in which the helicase and polymerase are moving in one-nucleotide steps, DNA synthesis drives fork unwinding, and a role of the helicase is to trap the unwound bases and prevent DNA reannealing.

Indexed as

Base PairingDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA ReplicationNucleotidesDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesNucleotides

Identifiers

PMID24630996
PMCPMC4010093
OpenAlexW2041245869

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.