Evidence map›Paper›PMID 24510100›Full record

ArticleNucleic acids research2014

Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.

Annika Butterer, Christian Pernstich, Rachel M Smith, Frank Sobott, Mark D Szczelkun, Júlia Tóth

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. How to Unmask an Unknown: The Restriction-Modification SystemInternational journal of molecular sciences · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Phylogenomics of Cas4 family nucleases.BMC evolutionary biology · 2017
    Article
  15. Review
  16. Article
  17. Evolutionary Ecology of Prokaryotic Immune Mechanisms.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  18. Article
  19. Review
  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

6 authors at 1 institution in 1 country.

Annika ButtererBiomolecular & Analytical Mass Spectrometry and Center for Proteomics (CFP-CeProMa), Department of Chemistry, University of Antwerp, Antwerp 2020, Belgium and DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Christian Pernstich
Rachel M Smith
Frank Sobott
Mark D Szczelkun
Júlia Tóth
University of Antwerp · BE

Funding

Wellcome Trust 078794Wellcome Trust 084086
6 · The paper itself

Abstract

Fundamental aspects of the biochemistry of Type III restriction endonucleases remain unresolved despite being characterized by numerous research groups in the past decades. One such feature is the subunit stoichiometry of these hetero-oligomeric enzyme complexes, which has important implications for the reaction mechanism. In this study, we present a series of results obtained by native mass spectrometry and size exclusion chromatography with multi-angle light scattering consistent with a 1:2 ratio of Res to Mod subunits in the EcoP15I, EcoPI and PstII complexes as the main holoenzyme species and a 1:1 stoichiometry of specific DNA (sDNA) binding by EcoP15I and EcoPI. Our data are also consistent with a model where ATP hydrolysis activated by recognition site binding leads to release of the enzyme from the site, dissociation from the substrate via a free DNA end and cleavage of the DNA. These results are discussed critically in the light of the published literature, aiming to resolve controversies and discuss consequences in terms of the reaction mechanism.

Indexed as

Adenosine TriphosphateDeoxyribonucleases, Type III Site-SpecificDNADNA Modification MethylasesHoloenzymesProtein MultimerizationProtein SubunitsSite-Specific DNA-Methyltransferase (Adenine-Specific)Adenosine TriphosphateDeoxyribonucleases, Type III Site-SpecificDNADNA modification methylase EcoP15IDNA modification methylase EcoPIDNA Modification MethylasesDNA restriction enzyme EcoPIendodeoxyribonuclease EcoP15IHoloenzymesProtein SubunitsSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID24510100
PMCPMC4005696
OpenAlexW2104449341

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.