Evidence map›Paper›PMID 20350931›Full record

ArticleNucleic acids research2010

Mechanism of sequence-specific template binding by the DNA primase of bacteriophage T7.

Seung-Joo Lee, Bin Zhu, Samir M Hamdan, Charles C Richardson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Primer release is the rate-limiting event in lagging-strand synthesis mediated by the T7 replisome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Choreography of bacteriophage T7 DNA replication.Current opinion in chemical biology · 2011
    Review
  19. Direct role for the RNA polymerase domain of T7 primase in primer delivery.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. Genome Analysis of an Enterococcal Prophage, Entfac.MY.Avicenna journal of medical biotechnology
    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

4 authors at 1 institution in 1 country.

Seung-Joo LeeDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Bin Zhu
Samir M Hamdan
Charles C Richardson
Harvard University · US

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

DNA primases catalyze the synthesis of the oligoribonucleotides required for the initiation of lagging strand DNA synthesis. Biochemical studies have elucidated the mechanism for the sequence-specific synthesis of primers. However, the physical interactions of the primase with the DNA template to explain the basis of specificity have not been demonstrated. Using a combination of surface plasmon resonance and biochemical assays, we show that T7 DNA primase has only a slightly higher affinity for DNA containing the primase recognition sequence (5'-TGGTC-3') than for DNA lacking the recognition site. However, this binding is drastically enhanced by the presence of the cognate Nucleoside triphosphates (NTPs), Adenosine triphosphate (ATP) and Cytosine triphosphate (CTP) that are incorporated into the primer, pppACCA. Formation of the dimer, pppAC, the initial step of sequence-specific primer synthesis, is not sufficient for the stable binding. Preformed primers exhibit significantly less selective binding than that observed with ATP and CTP. Alterations in subdomains of the primase result in loss of selective DNA binding. We present a model in which conformational changes induced during primer synthesis facilitate contact between the zinc-binding domain and the polymerase domain.

Indexed as

Adenosine TriphosphateBacteriophage T7Base SequenceBinding SitesCytidine TriphosphateDNA-Binding ProteinsDNA PrimaseDNA, Single-StrandedModels, MolecularOligoribonucleotidesProtein BindingProtein Structure, TertiaryTemplates, GeneticAdenosine TriphosphateCytidine TriphosphateDNA-Binding ProteinsDNA PrimaseDNA, Single-StrandedOligoribonucleotides

Identifiers

PMID20350931
PMCPMC2910064
OpenAlexW2079881378

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.