Evidence map›Paper›PMID 21651304›Full record

ArticleBiochemistry2011

Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a first step in lesion detection.

Christine A Romano, Pamela A Sontz, Jacqueline K Barton

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Sensing DNA through DNA Charge Transport.ACS chemical biology · 2018
    Review
  9. Article
  10. Electrical Probes of DNA-Binding Proteins.Methods in enzymology · 2017
    Article
  11. Redox Signaling through DNA.Israel journal of chemistry · 2016
    Article
  12. Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe-2S cluster.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Review
  14. Low-intensity red and infrared laser effects at high fluences on Escherichia coli cultures.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2015
    Article
  15. Article
  16. Review
  17. Multiplexed electrochemistry of DNA-bound metalloproteins.Journal of the American Chemical Society · 2013
    Article
  18. DNA helicases associated with genetic instability, cancer, and aging.Advances in experimental medicine and biology · 2013
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Christine A RomanoDivision of Chemistry and Chemical Engineering, California Institute of Technolog, Pasadena, California 91125, USA.
Pamela A Sontz
Jacqueline K Barton
California Institute of Technology · US

Funding

DNA-MEDIATED ELECTRON TRANSFER REACTIONSR01GM049216 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BARTON, JACQUELINE K · 1993 to 2012
$4.0M
NIGMS NIH HHS GM49216NIGMS NIH HHS R01 GM049216
6 · The paper itself

Abstract

Endonuclease III (EndoIII) is a base excision repair glycosylase that targets damaged pyrimidines and contains a [4Fe-4S] cluster. We have proposed a model where BER proteins that contain redox-active [4Fe-4S] clusters utilize DNA charge transport (CT) as a first step in the detection of DNA lesions. Here, several mutants of EndoIII were prepared to probe their efficiency of DNA/protein charge transport. Cyclic voltammetry experiments on DNA-modified electrodes show that aromatic residues F30, Y55, Y75, and Y82 help mediate charge transport between DNA and the [4Fe-4S] cluster. On the basis of circular dichroism studies to measure protein stability, mutations at residues W178 and Y185 are found to destabilize the protein; these residues may function to protect the [4Fe-4S] cluster. Atomic force microscopy studies furthermore reveal a correlation in the ability of mutants to carry out protein/DNA CT and their ability to relocalize onto DNA strands containing a single base mismatch; EndoIII mutants that are defective in carrying out DNA/protein CT do not redistribute onto mismatch-containing strands, consistent with our model. These results demonstrate a link between the ability of the repair protein to carry out DNA CT and its ability to relocalize near lesions, thus pointing to DNA CT as a key first step in the detection of base damage in the genome.

Indexed as

Mutagenesis, Site-DirectedBase Pair MismatchDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA DamageDNA GlycosylasesDNA RepairElectrochemistryEscherichia coliEscherichia coli ProteinsIron-Sulfur ProteinsMicroscopy, Atomic ForceOxidation-ReductionProtein TransportSignal TransductionDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA GlycosylasesEscherichia coli ProteinsIron-Sulfur ProteinsmutY adenine glycosylaseNTH protein, E coli

Identifiers

PMID21651304
PMCPMC3134277
OpenAlexW1978833946

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.