Evidence map›Paper›PMID 26620561›Full record

ArticleThe Journal of biological chemistry2016

Binding Affinities among DNA Helicase-Primase, DNA Polymerase, and Replication Intermediates in the Replisome of Bacteriophage T7.

Huidong Zhang, Yong Tang, Seung-Joo Lee, Zeliang Wei, Jia Cao, Charles C Richardson

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

6 citing papers in PubMed, 22 citations in OpenAlex.

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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 2 institutions in 2 countries.

Huidong ZhangFrom the Institute of Toxicology, College of Preventive Medicine, Third Military Medical University, Chongqing 400038, China and the Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boson, Massachusetts 02115 huidongzhang@tmmu.edu.cn.
Yong TangFrom the Institute of Toxicology, College of Preventive Medicine, Third Military Medical University, Chongqing 400038, China and.
Seung-Joo Leethe Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boson, Massachusetts 02115.
Zeliang WeiFrom the Institute of Toxicology, College of Preventive Medicine, Third Military Medical University, Chongqing 400038, China and.
Jia CaoFrom the Institute of Toxicology, College of Preventive Medicine, Third Military Medical University, Chongqing 400038, China and.
Charles C Richardsonthe Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boson, Massachusetts 02115 ccr@hms.harvard.edu.
Army Medical University · CNHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of a replication loop on the lagging strand facilitates coordinated synthesis of the leading- and lagging-DNA strands and provides a mechanism for recycling of the lagging-strand DNA polymerase. As an Okazaki fragment is completed, the loop is released, and a new loop is formed as the synthesis of a new Okazaki fragment is initiated. Loop release requires the dissociation of the complex formed by the interactions among helicase, DNA polymerase, and DNA. The completion of the Okazaki fragment may result in either a nick or a single-stranded DNA region. In the replication system of bacteriophage T7, the dissociation of the polymerase from either DNA region is faster than that observed for the dissociation of the helicase from DNA polymerase, implying that the replication loop is released more likely through the dissociation of the lagging-strand DNA from polymerase, retaining the polymerase at replication fork. Both dissociation of DNA polymerase from DNA and that of helicase from a DNA polymerase · DNA complex are much faster at a nick DNA region than the release from a ssDNA region. These results suggest that the replication loop is released as a result of the nick formed when the lagging-strand DNA polymerase encounters the previously synthesized Okazaki fragment, releasing lagging-strand DNA and retaining DNA polymerase at the replication fork for the synthesis of next Okazaki fragment.

Indexed as

DNA ReplicationModels, MolecularBacteriophage T7Binding SitesDNADNA, BacterialDNA-Directed DNA PolymeraseDNA PrimaseDNA, Single-StrandedDNA, ViralEscherichia coliEscherichia coli ProteinsGene DeletionKineticsMultienzyme ComplexesNucleic Acid Conformationbacteriophage T7 induced DNA polymeraseDNADNA, BacterialDNA-Directed DNA PolymeraseDNA PrimaseDNA, Single-StrandedDNA, ViralEscherichia coli ProteinsMultienzyme ComplexesOkazaki fragmentsRecombinant ProteinsReplisomesThioredoxinsTrxA protein, E coliViral ProteinsbacteriophageDNA-protein interactionDNA replicationenzyme kineticspre-steady-state kinetics

Identifiers

PMID26620561
PMCPMC4714229
OpenAlexW2181384562

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.