Evidence map›Paper›PMID 24368349›Full record

ArticleBiochimica et biophysica acta2014

ArdA proteins from different mobile genetic elements can bind to the EcoKI Type I DNA methyltransferase of E. coli K12.

Kai Chen, Marcel Reuter, Bansi Sanghvi, Gareth A Roberts, Laurie P Cooper, Matthew Tilling, Garry W Blakely, David T F Dryden

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 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
0.5field-weighted citation impact, top 29% 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, 26 citations in OpenAlex.

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  19. Anti-Restriction Protein, KlcAFrontiers in cellular and infection microbiology · 2017
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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

8 authors at 1 institution in 1 country.

Kai ChenEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Marcel ReuterEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Bansi SanghviEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Gareth A RobertsEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Laurie P CooperEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Matthew TillingEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
Garry W BlakelyInstitute of Cell Biology, School of Biological Sciences, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JR, UK.
David T F DrydenEaStCHEM School of Chemistry, The University of Edinburgh, The King's Buildings, Edinburgh EH9 3JJ, UK.
University of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C511599/1Biotechnology and Biological Sciences Research Council BB/D001870/1Wellcome TrustWellcome Trust 090288/Z/09/ZAWellcome Trust GR080463MA
6 · The paper itself

Abstract

Anti-restriction and anti-modification (anti-RM) is the ability to prevent cleavage by DNA restriction-modification (RM) systems of foreign DNA entering a new bacterial host. The evolutionary consequence of anti-RM is the enhanced dissemination of mobile genetic elements. Homologues of ArdA anti-RM proteins are encoded by genes present in many mobile genetic elements such as conjugative plasmids and transposons within bacterial genomes. The ArdA proteins cause anti-RM by mimicking the DNA structure bound by Type I RM enzymes. We have investigated ArdA proteins from the genomes of Enterococcus faecalis V583, Staphylococcus aureus Mu50 and Bacteroides fragilis NCTC 9343, and compared them to the ArdA protein expressed by the conjugative transposon Tn916. We find that despite having very different structural stability and secondary structure content, they can all bind to the EcoKI methyltransferase, a core component of the EcoKI Type I RM system. This finding indicates that the less structured ArdA proteins become fully folded upon binding. The ability of ArdA from diverse mobile elements to inhibit Type I RM systems from other bacteria suggests that they are an advantage for transfer not only between closely-related bacteria but also between more distantly related bacterial species.

Indexed as

Interspersed Repetitive SequencesChromatography, GelCircular DichroismEscherichia coli K12Escherichia coli ProteinsModels, MolecularProtein BindingProtein DenaturationProtein Structure, SecondaryRepressor ProteinsSite-Specific DNA-Methyltransferase (Adenine-Specific)ArdA protein, E coliDNA modification methylase EcoKIEscherichia coli ProteinsRepressor ProteinsSite-Specific DNA-Methyltransferase (Adenine-Specific)ArdA proteinDNA methyltransferaseDNA mimicHorizontal gene transfer

Identifiers

PMID24368349
PMCPMC3969726
OpenAlexW2034842656

What OpenQuestion holds

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Registered trials

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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.