Evidence map›Paper›PMID 23947567›Full record

ArticleChemical research in toxicology2013

Ring-opening of the γ-OH-PdG adduct promotes error-free bypass by the Sulfolobus solfataricus DNA polymerase Dpo4.

Ganesh Shanmugam, Irina G Minko, Surajit Banerjee, Plamen P Christov, Ivan D Kozekov, Carmelo J Rizzo, R Stephen Lloyd, Martin Egli, Michael P Stone

Abstract read
In one paragraph

Article in Chemical research in toxicology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review
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

9 authors at 4 institutions in 1 country.

Ganesh ShanmugamDepartment of Chemistry, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt Institute of Chemical Biology, and Center for Structural Biology, Vanderbilt University , Nashville, Tennessee 37235, United States.
Irina G Minko
Surajit Banerjee
Plamen P Christov
Ivan D Kozekov
Carmelo J Rizzo
R Stephen Lloyd
Martin Egli
Michael P Stone
Vanderbilt University · USOregon Health & Science University · USArgonne National Laboratory · USCornell University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
Synthetic Approaches to Carcinogen-Linked OligonucleotidesP01CA160032 · NCI · VANDERBILT UNIVERSITY · PI STONE, MICHAEL P · 2012 to 2022
$14.0M
SYNTHETIC APPROACHES TO PAH-ADDUCTED NUCLEOTIDESP01ES005355 · NIEHS · VANDERBILT UNIVERSITY · PI LLOYD, STEPHEN CARROLL · 1991 to 2010
$13.4M
NCI NIH HHS P01 CA160032NCI NIH HHS P30 CA068485NIEHS NIH HHS P01 ES05355NIEHS NIH HHS P30 ES000267NIEHS NIH HHS P30 ES00267
6 · The paper itself

Abstract

Acrolein, a mutagenic aldehyde, reacts with deoxyguanosine (dG) to form 3-(2'-deoxy-β-d-erythro-pentofuranosyl)-5,6,7,8-tetrahydro-8-hydroxypyrimido[1,2-a] purin-10(3H)-one (γ-OH-PdG). When placed opposite deoxycytosine (dC) in DNA, γ-OH-PdG undergoes ring-opening to the N(2)-(3-oxopropyl)-dG. Ring-opening of the adduct has been hypothesized to facilitate nonmutagenic bypass, particularly by DNA polymerases of the Y family. This study examined the bypass of γ-OH-PdG by Sulfolobus solfataricus Dpo4, the prototypic Y-family DNA polymerase, using templates that contained the adduct in either the 5'-CXG-3' or the 5'-TXG-3' sequence context. Although γ-OH-PdG partially blocked Dpo4-catalyzed DNA synthesis, full primer extension was observed, and the majority of bypass products were error-free. Conversion of the adduct into an irreversibly ring-opened derivative prior to reaction facilitated bypass and further improved the fidelity. Structures of ternary Dpo4·DNA·dNTP complexes were determined with primers that either were positioned immediately upstream of the lesion (preinsertion complexes) or had a 3'-terminal dC opposite the lesion (postinsertion complexes); the incoming nucleotides, either dGTP or dATP, were complementary to the template 5'-neighbor nucleotide. In both postinsertion complexes, the adduct existed as ring-opened species, and the resulting base-pair featured Watson-Crick hydrogen bonding. The incoming nucleotide paired with the 5'-neighbor template, while the primer 3'-hydroxyl was positioned to facilitate extension. In contrast, γ-OH-PdG was in the ring-closed form in both preinsertion complexes, and the overall structure did not favor catalysis. These data provide insights into γ-OH-PdG chemistry during replication bypass by the Dpo4 DNA polymerase and may explain why γ-OH-PdG-induced mutations due to primer-template misalignment are uncommon.

Indexed as

Crystallography, X-RayDeoxyguanosineDNA AdductsDNA Polymerase betaModels, MolecularMolecular StructureSulfolobus solfataricus3-(2-deoxypentofuranosyl)-5,6,7,8-tetrahydro-8-hydroxy-6-tridecylpyrimido(1,2-a)purine-10(3H)oneDeoxyguanosineDNA AdductsDNA Polymerase beta

Identifiers

PMID23947567
PMCPMC3775444
OpenAlexW2151826086

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.