Evidence map›Paper›PMID 22977246›Full record

ArticleThe Journal of biological chemistry2012

An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome.

Arkadiusz W Kulczyk, Barak Akabayov, Seung-Joo Lee, Mihnea Bostina, Steven A Berkowitz, Charles C Richardson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. IBPred: A sequence-based predictor for identifying ion binding protein in phage.Computational and structural biotechnology journal · 2022
    Article
  3. Article
  4. DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. T7 replisome directly overcomes DNA damage.Nature communications · 2015
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Bacteriophage T7 DNA polymerase - sequenase.Frontiers in microbiology · 2014
    Review
  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

6 authors at 3 institutions in 2 countries.

Arkadiusz W KulczykDepartment of Biological Chemistry and Molecular Pharmacology, Harvard University Medical School, Boston, Massachusetts 02115, USA.
Barak Akabayov
Seung-Joo Lee
Mihnea Bostina
Steven A Berkowitz
Charles C Richardson
Harvard University · USBiogen (United States) · USMcGill University · CA

Funding

STRUCTURE AND SYNTHESIS OF DNAR01GM054397 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RICHARDSON, CHARLES C. · 1996 to 2011
$7.6M
NIGMS NIH HHS GM-54397NIGMS NIH HHS R01 GM054397
6 · The paper itself

Abstract

Synthesis of the leading DNA strand requires the coordinated activity of DNA polymerase and DNA helicase, whereas synthesis of the lagging strand involves interactions of these proteins with DNA primase. We present the first structural model of a bacteriophage T7 DNA helicase-DNA polymerase complex using a combination of small angle x-ray scattering, single-molecule, and biochemical methods. We propose that the protein-protein interface stabilizing the leading strand synthesis involves two distinct interactions: a stable binding of the helicase to the palm domain of the polymerase and an electrostatic binding of the carboxyl-terminal tail of the helicase to a basic patch on the polymerase. DNA primase facilitates binding of DNA helicase to ssDNA and contributes to formation of the DNA helicase-DNA polymerase complex by stabilizing DNA helicase.

Indexed as

Virus ReplicationBacteriophage T7CatalysisDNA-Directed DNA PolymeraseDNA HelicasesDNA ReplicationDNA, Single-StrandedKineticsMicroscopy, ElectronModels, MolecularProtein ConformationProtein Structure, TertiaryScattering, RadiationSurface Plasmon ResonanceUltracentrifugationViral ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA, Single-StrandedViral Proteins

Identifiers

PMID22977246
PMCPMC3493946
OpenAlexW1977772055

What OpenQuestion holds

Textmetadata
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.