Evidence map›Paper›PMID 27002236›Full record

ArticleBiochemistry2016

Single-Molecule Investigation of Response to Oxidative DNA Damage by a Y-Family DNA Polymerase.

Austin T Raper, Varun V Gadkari, Brian A Maxwell, Zucai Suo

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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Beyond the Lesion: Back to High Fidelity DNA Synthesis.Frontiers in molecular biosciences · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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.

Austin T RaperDepartment of Chemistry and Biochemistry, †Ohio State Biochemistry Program and ‡Ohio State Biophysics Program, The Ohio State University , Columbus, Ohio 43210, United States.
Varun V GadkariDepartment of Chemistry and Biochemistry, †Ohio State Biochemistry Program and ‡Ohio State Biophysics Program, The Ohio State University , Columbus, Ohio 43210, United States.
Brian A MaxwellDepartment of Chemistry and Biochemistry, †Ohio State Biochemistry Program and ‡Ohio State Biophysics Program, The Ohio State University , Columbus, Ohio 43210, United States.
Zucai SuoDepartment of Chemistry and Biochemistry, †Ohio State Biochemistry Program and ‡Ohio State Biophysics Program, The Ohio State University , Columbus, Ohio 43210, United States.

Funding

CHEMISTRY/BIOLOGY TRAINING GRANTT32GM008512 · NIGMS · OHIO STATE UNIVERSITY · PI PEI, DEHUA · 1996 to 2016
$3.9M
BIOLOGICAL EFFECTS OF DNA ADDUCTS FORMED BY NITROPYRENESR01ES009127 · NIEHS · UNIVERSITY OF CONNECTICUT STORRS · PI BASU, ASHIS K, SUO, ZUCAI · 1998 to 2014
$3.5M
Biological Effects of DNA Adducts Formed by Nitroaromatic CompoundsR56ES009127 · NIEHS · UNIVERSITY OF CONNECTICUT STORRS · PI BASU, ASHIS K, SUO, ZUCAI · 2009 to 2009
$393k
NIEHS NIH HHS ES009127NIEHS NIH HHS R01 ES009127NIEHS NIH HHS R56 ES009127NIGMS NIH HHS T32 GM008512NIGMS NIH HHS T32GM008512
6 · The paper itself

Abstract

Y-family DNA polymerases are known to bypass DNA lesions in vitro and in vivo and rescue stalled DNA replication machinery. Dpo4, a well-characterized model Y-family DNA polymerase, is known to catalyze translesion synthesis across a variety of DNA lesions including 8-oxo-7,8-dihydro-2'-deoxyguanine (8-oxo-dG). Our previous X-ray crystallographic, stopped-flow Förster resonance energy transfer (FRET), and computational simulation studies have revealed that Dpo4 samples a variety of global conformations as it recognizes and binds DNA. Here we employed single-molecule FRET (smFRET) techniques to investigate the kinetics and conformational dynamics of Dpo4 when it encountered 8-oxo-dG, a major oxidative lesion with high mutagenic potential. Our smFRET data indicated that Dpo4 bound the DNA substrate in multiple conformations, as suggested by three observed FRET states. An incoming correct or incorrect nucleotide affected the distribution and stability of these states with the correct nucleotide completely shifting the equilibrium toward a catalytically competent complex. Furthermore, the presence of the 8-oxo-dG lesion in the DNA stabilized both the binary and ternary complexes of Dpo4. Thus, our smFRET analysis provided a basis for the enhanced efficiency which Dpo4 is known to exhibit when replicating across from 8-oxo-dG.

Indexed as

DNA DamageDNA RepairModels, MolecularProtein Engineering8-Hydroxy-2'-DeoxyguanosineAmino Acid SubstitutionArchaeal ProteinsComputer SimulationDeoxyguanosineDNA Polymerase betaFluorescence Resonance Energy TransferMutationOxidation-ReductionProtein ConformationProtein RefoldingProtein Stability8-Hydroxy-2'-DeoxyguanosineArchaeal ProteinsDeoxyguanosineDNA Polymerase betaRecombinant Proteins

Identifiers

PMID27002236
PMCPMC5026495

What OpenQuestion holds

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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.