Evidence map›Paper›PMID 25899385›Full record

ArticleThe FEBS journal2015

Noncognate DNA damage prevents the formation of the active conformation of the Y-family DNA polymerases DinB and DNA polymerase κ.

Philip Nevin, Xueguang Lu, Ke Zhang, John R Engen, Penny J Beuning

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Mammalian DNA Polymerase Kappa Activity and Specificity.Molecules (Basel, Switzerland) · 2019
    Review
  7. Article
  8. Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018
    Article
  9. Observational
  10. Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

5 authors at 1 institution in 1 country.

Philip NevinDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
Xueguang LuDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
Ke ZhangDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
Penny J BeuningDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
Northeastern University · US

Funding

Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM101135NIGMS NIH HHS R01-GM101135
6 · The paper itself

Abstract

Y-family DNA polymerases are specialized to copy damaged DNA, and are associated with increased mutagenesis, owing to their low fidelity. It is believed that the mechanism of nucleotide selection by Y-family DNA polymerases involves conformational changes preceding nucleotidyl transfer, but there is limited experimental evidence for such structural changes. In particular, nucleotide-induced conformational changes in bacterial or eukaryotic Y-family DNA polymerases have, to date, not been extensively characterized. Using hydrogen-deuterium exchange mass spectrometry, we demonstrate here that the Escherichia coli Y-family DNA polymerase DinB and its human ortholog DNA polymerase κ undergo a conserved nucleotide-induced conformational change in the presence of undamaged DNA and the correct incoming nucleotide. Notably, this holds true for damaged DNA containing N(2) -furfuryl-deoxyguanosine, which is efficiently copied by these two polymerases, but not for damaged DNA containing the major groove modification O(6) -methyl-deoxyguanosine, which is a poor substrate. Our observations suggest that DinB and DNA polymerase κ utilize a common mechanism for nucleotide selection involving a conserved prechemical conformational transition promoted by the correct nucleotide and only preferred DNA substrates.

Indexed as

Deuterium Exchange MeasurementDNA DamageDNA-Directed DNA PolymeraseEscherichia coli ProteinsGuanineProtein ConformationY-Family DNA PolymerasesDinB protein, E coliDNA-Directed DNA PolymeraseEscherichia coli ProteinsGuanineO-(6)-methylguaninePOLK protein, humanY-Family DNA Polymerasesconformational changeDNA replicationhydrogen exchange mass spectrometrynucleotide selectionsubstrate specificity

Identifiers

PMID25899385
PMCPMC4504746
OpenAlexW2147814294

What OpenQuestion holds

Textmetadata
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.