Evidence map›Paper›PMID 27096230›Full record

ArticleBiochemistry2016

Effect of Different Divalent Cations on the Kinetics and Fidelity of RB69 DNA Polymerase.

Ashwani Kumar Vashishtha, William H Konigsberg

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  3. A wide survey of heavy metals-inducedCurrent research in toxicology · 2024
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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

2 authors at 1 institution in 1 country.

Ashwani Kumar VashishthaDepartment of Molecular Biophysics and Biochemistry, Yale University , New Haven, Connecticut 06520-8024, United States.
William H KonigsbergDepartment of Molecular Biophysics and Biochemistry, Yale University , New Haven, Connecticut 06520-8024, United States.
Yale University · US

Funding

Molecular Biology and Structure of a DNA ReplicaseR01GM063276 · NIGMS · YALE UNIVERSITY · PI KONIGSBERG, WILLIAM H · 2001 to 2013
$4.2M
NIGMS NIH HHS R01 GM063276
6 · The paper itself

Abstract

Although Mg(2+) is the cation that functions as the cofactor for the nucleotidyl transfer reaction for almost all DNA polymerases, Mn(2+) can also serve, but when it does, the degree of base discrimination exhibited by most DNA polymerases (pols) is diminished. Metal ions other than Mg(2+) or Mn(2+) can also act as cofactors depending on the specific DNA polymerase. Here, we tested the ability of several divalent metal ions to substitute for Mg(2+) or Mn(2+) with RB69 DNA polymerase (RB69pol), a model B-family pol. Our choice of metal ions was based on previous studies with other DNA pols. Co(2+), and to a lesser extent Ni(2+), were the only cations among those tested besides Mg(2+) and Mn(2+) that could serve as cofactors with RB69pol. The incorporation efficiency of correct dNMPs increased by 5-fold with Co(2+), relative to that of Mg(2+). The incorporation efficiencies of incorrect dNMPs increased by 2-17-fold with Co(2+), relative to that with Mg(2+) depending on the incoming dNTP. Base selectivity was reduced even further with Mn(2+) compared to that observed with Co(2+). Substitution of Mn(2+), Co(2+), or Ni(2+) for Mg(2+) reduced the exonuclease activity of RB69pol by 2-, 6-, and 33-fold, respectively, contributing to the frequency of misincorporation. In addition, Co(2+) and Mn(2+) were better able to extend a primer past a mismatch than Mg(2+). Finally, Co(2+) and Mn(2+) enhanced ground-state binding of both correct and incorrect dNTPs to RB69pol:dideoxy-terminated primer-template complexes.

Indexed as

BacteriophagesBinding SitesCations, DivalentCobaltDNA-Directed DNA PolymeraseEscherichia coliMagnesiumManganeseNucleotidesProtein BindingViral Proteinsbacteriophage RB69 DNA polymeraseCations, DivalentCobaltDNA-Directed DNA PolymeraseMagnesiumManganeseNucleotidesViral Proteins

Identifiers

PMID27096230
PMCPMC5989577
OpenAlexW2338423859

What OpenQuestion holds

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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.