Evidence map›Paper›PMID 34188055›Full record

ArticleNature communications2021

Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymerase.

Olga Rechkoblit, Robert E Johnson, Yogesh K Gupta, Louise Prakash, Satya Prakash, Aneel K Aggarwal

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol.International journal of molecular sciences · 2025
    Article
  5. Article
  6. 8-Oxoadenine: A «New» Player of the Oxidative Stress in Mammals?International journal of molecular sciences · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. 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

6 authors.

Olga RechkoblitDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. olga.rechkoblit@mssm.edu.ORCID 0000-0003-4270-7242
Robert E JohnsonDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Yogesh K GuptaDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0001-6372-5007
Louise PrakashDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Satya PrakashDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Aneel K AggarwalDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. aneel.agarwal@mssm.edu.ORCID 0000-0003-4389-0173

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structure and Specificity of Restriction-Modification (R-M) SystemsR35GM131780 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ANEEL K. AGGARWAL · 2019 to 2026
$3.4M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Structure and function of DNA polymerase lambda opposite DNA lesions which disrupt Watson-Crick base pairingR01GM126087 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI PRAKASH, LOUISE · 2018 to 2021
$1.0M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM126087NIGMS NIH HHS R35 GM131780
6 · The paper itself

Abstract

PrimPol is a human DNA polymerase-primase that localizes to mitochondria and nucleus and bypasses the major oxidative lesion 7,8-dihydro-8-oxoguanine (oxoG) via translesion synthesis, in mostly error-free manner. We present structures of PrimPol insertion complexes with a DNA template-primer and correct dCTP or erroneous dATP opposite the lesion, as well as extension complexes with C or A as a 3'-terminal primer base. We show that during the insertion of C and extension from it, the active site is unperturbed, reflecting the readiness of PrimPol to accommodate oxoG(anti). The misinsertion of A opposite oxoG(syn) also does not alter the active site, and is likely less favorable due to lower thermodynamic stability of the oxoG(syn)•A base-pair. During the extension step, oxoG(syn) induces an opening of its base-pair with A or misalignment of the 3'-A primer terminus. Together, the structures show how PrimPol accurately synthesizes DNA opposite oxidatively damaged DNA in human cells.

Indexed as

Base PairingDNA DamageDNA-Directed DNA PolymeraseDNA PrimaseDNA ReplicationGuanineHumansMitochondriaMultifunctional EnzymesOxidative StressProtein ConformationReactive Oxygen Species7,8-dihydro-8-oxoguanineDNA-Directed DNA PolymeraseDNA PrimaseGuanineMultifunctional EnzymesPrimPol protein, humanReactive Oxygen Species

Identifiers

PMID34188055
PMCPMC8241999

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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.