Evidence map›Paper›PMID 19223329›Full record

ArticleNucleic acids research2009

Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping.

Kelly J Neaves, Laurie P Cooper, John H White, Stewart M Carnally, David T F Dryden, J Michael Edwardson, Robert M Henderson

Abstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Direct evidence for functional TRPV1/TRPA1 heteromers.Pflugers Archiv : European journal of physiology · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors.

Kelly J NeavesDepartment of Pharmacology, University of Cambridge, Cambridge, UK.
Laurie P Cooper
John H White
Stewart M Carnally
David T F Dryden
J Michael Edwardson
Robert M Henderson

Funding

Biotechnology and Biological Sciences Research Council BB/D001870/1Biotechnology and Biological Sciences Research Council BBS/B/1065XWellcome Trust GR080463MA
6 · The paper itself

Abstract

Atomic force microscopy (AFM) allows the study of single protein-DNA interactions such as those observed with the Type I Restriction-Modification systems. The mechanisms employed by these systems are complicated and understanding them has proved problematic. It has been known for years that these enzymes translocate DNA during the restriction reaction, but more recent AFM work suggested that the archetypal EcoKI protein went through an additional dimerization stage before the onset of translocation. The results presented here extend earlier findings confirming the dimerization. Dimerization is particularly common if the DNA molecule contains two EcoKI recognition sites. DNA loops with dimers at their apex form if the DNA is sufficiently long, and also form in the presence of ATPgammaS, a non-hydrolysable analogue of the ATP required for translocation, indicating that the looping is on the reaction pathway of the enzyme. Visualization of specific DNA loops in the protein-DNA constructs was achieved by improved sample preparation and analysis techniques. The reported dimerization and looping mechanism is unlikely to be exclusive to EcoKI, and offers greater insight into the detailed functioning of this and other higher order assemblies of proteins operating by bringing distant sites on DNA into close proximity via DNA looping.

Indexed as

Adenosine TriphosphateBinding SitesData Interpretation, StatisticalDimerizationDNADNA Restriction EnzymesMicroscopy, Atomic ForceProtein BindingProtein MultimerizationSite-Specific DNA-Methyltransferase (Adenine-Specific)adenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphateDNADNA modification methylase EcoKIDNA Restriction Enzymesendodeoxyribonuclease EcoKISite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID19223329
PMCPMC2665228

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.