Evidence map›Paper›PMID 24062430›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Single-molecule FRET and linear dichroism studies of DNA breathing and helicase binding at replication fork junctions.

Carey Phelps, Wonbae Lee, Davis Jose, Peter H von Hippel, Andrew H Marcus

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

57 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Linear Dichroism Measurements for the Study of Protein-DNA Interactions.International journal of molecular sciences · 2023
    Review
  11. Examining DNA breathing with pyDNA-EPBD.Bioinformatics (Oxford, England) · 2023
    Article
  12. Article
  13. Review
  14. "Helicase" Activity promoted through dynamic interactions between a ssDNA translocase and a diffusing SSB protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Bubble Relaxation Dynamics in Homopolymer DNA Sequences.Molecules (Basel, Switzerland) · 2023
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Carey PhelpsOregon Center for Optics, Department of Chemistry and Biochemistry, and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403.
Wonbae Lee
Davis Jose
Peter H von Hippel
Andrew H Marcus
University of Oregon · US

Funding

STRUCTURE AND RELATIONS OF PROTEINS AND NUCLEIC ACIDSR01GM015792 · NIGMS · UNIVERSITY OF OREGON · PI MARCUS, ANDREW HADLEY · 1985 to 2025
$10.2M
STRUCTURE &RELATIONS OF PROTEINS &NUCLEIC ACIDSR37GM015792 · NIGMS · UNIVERSITY OF OREGON · PI VON HIPPEL, PETER HANS · 1988 to 1997
–
NIGMS NIH HHS GM-15792NIGMS NIH HHS R01 GM015792
6 · The paper itself

Abstract

DNA "breathing" is a thermally driven process in which base-paired DNA sequences transiently adopt local conformations that depart from their most stable structures. Polymerases and other proteins of genome expression require access to single-stranded DNA coding templates located in the double-stranded DNA "interior," and it is likely that fluctuations of the sugar-phosphate backbones of dsDNA that result in mechanistically useful local base pair opening reactions can be exploited by such DNA regulatory proteins. Such motions are difficult to observe in bulk measurements, both because they are infrequent and because they often occur on microsecond time scales that are not easy to access experimentally. We report single-molecule fluorescence experiments with polarized light, in which tens-of-microseconds rotational motions of internally labeled iCy3/iCy5 donor-acceptor Förster resonance energy transfer fluorophore pairs that have been rigidly inserted into the backbones of replication fork constructs are simultaneously detected using single-molecule Förster resonance energy transfer and single-molecule fluorescence-detected linear dichroism signals. Our results reveal significant local motions in the ∼100-μs range, a reasonable time scale for DNA breathing fluctuations of potential relevance for DNA-protein interactions. Moreover, we show that both the magnitudes and the relaxation times of these backbone breathing fluctuations are significantly perturbed by interactions of the fork construct with a nonprocessive, weakly binding bacteriophage T4-coded helicase hexamer initiation complex, suggesting that these motions may play a fundamental role in the initial binding, assembly, and function of the processive helicase-primase (primosome) component of the bacteriophage T4-coded DNA replication complex.

Indexed as

DNA ReplicationAlgorithmsBacteriophage T4CarbocyaninesDNADNA, Single-StrandedDNA, ViralFluorescence Resonance Energy TransferFluorescent DyesKineticsModels, GeneticModels, MolecularNucleic Acid ConformationProtein MultimerizationViral ProteinsCarbocyaninescyanine dye 3cyanine dye 5DNADNA, Single-StrandedDNA, ViralFluorescent Dyesgene 41 protein, Enterobacteria phage T4Viral ProteinsDNA helicasesingle-molecule linear dichroismsmFRETT4 primosome helicasethermal fluctuations

Identifiers

PMID24062430
PMCPMC3808625
OpenAlexW2115634861

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.