Evidence map›Paper›PMID 30165537›Full record

ArticleNucleic acids research2018

A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes.

Edward K M Bower, Laurie P Cooper, Gareth A Roberts, John H White, Yvette Luyten, Richard D Morgan, David T F Dryden

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Bacterial immune systems.Antonie van Leeuwenhoek · 2026
    Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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 at 3 institutions in 2 countries.

Edward K M BowerEaStCHEM School of Chemistry, University of Edinburgh, The King's Buildings, Edinburgh EH9 3FJ, UK.
Laurie P CooperEaStCHEM School of Chemistry, University of Edinburgh, The King's Buildings, Edinburgh EH9 3FJ, UK.
Gareth A RobertsEaStCHEM School of Chemistry, University of Edinburgh, The King's Buildings, Edinburgh EH9 3FJ, UK.
John H WhiteEaStCHEM School of Chemistry, University of Edinburgh, The King's Buildings, Edinburgh EH9 3FJ, UK.
Yvette LuytenNew England Biolabs, 240 County Road, Ipswich, MA 01938-2723, USA.
Richard D MorganNew England Biolabs, 240 County Road, Ipswich, MA 01938-2723, USA.
David T F DrydenDepartment of Biosciences, Durham University, South Road, Durham DH1 3LE, UK.
University of Edinburgh · GBNew England Biolabs (United States) · USDurham University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Restriction Modification (RM) systems prevent the invasion of foreign genetic material into bacterial cells by restriction and protect the host's genetic material by methylation. They are therefore important in maintaining the integrity of the host genome. RM systems are currently classified into four types (I to IV) on the basis of differences in composition, target recognition, cofactors and the manner in which they cleave DNA. Comparing the structures of the different types, similarities can be observed suggesting an evolutionary link between these different types. This work describes the 'deconstruction' of a large Type I RM enzyme into forms structurally similar to smaller Type II RM enzymes in an effort to elucidate the pathway taken by Nature to form these different RM enzymes. Based upon the ability to engineer new enzymes from the Type I 'scaffold', an evolutionary pathway and the evolutionary pressures required to move along the pathway from Type I RM systems to Type II RM systems are proposed. Experiments to test the evolutionary model are discussed.

Indexed as

Evolution, MolecularModels, GeneticAmino Acid SequenceBinding SitesDeoxyribonucleases, Type II Site-SpecificDeoxyribonucleases, Type I Site-SpecificDNA, BacterialEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein Interaction Domains and MotifsDeoxyribonucleases, Type II Site-SpecificDeoxyribonucleases, Type I Site-SpecificDNA, BacterialEscherichia coli ProteinsHsdR protein, E colihsdS protein, E coli

Identifiers

PMID30165537
PMCPMC6158711
OpenAlexW2888836250

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.