Evidence map›Paper›PMID 19506028›Full record

ArticleNucleic acids research2009

Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance.

Stephen A McMahon, Gareth A Roberts, Kenneth A Johnson, Laurie P Cooper, Huanting Liu, John H White, Lester G Carter, Bansi Sanghvi, Muse Oke, Malcolm D Walkinshaw and 3 more

Open access · goldAbstract 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 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

81 citing papers in PubMed, 122 citations in OpenAlex.

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21 more citing papers are in PubMed but not listed here.

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

13 authors at 2 institutions in 1 country.

Stephen A McMahonCentre for Biomolecular Science, The University, St Andrews KY16 9ST, UK.
Gareth A Roberts
Kenneth A Johnson
Laurie P Cooper
Huanting Liu
John H White
Lester G Carter
Bansi Sanghvi
Muse Oke
Malcolm D Walkinshaw
Garry W Blakely
James H Naismith
David T F Dryden
University of Edinburgh · GBUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001870/1Biotechnology and Biological Sciences Research Council BB/D522589/1Biotechnology and Biological Sciences Research Council BB/S/B14450Wellcome Trust 080463Wellcome Trust GR080463MA
6 · The paper itself

Abstract

The ardA gene, found in many prokaryotes including important pathogenic species, allows associated mobile genetic elements to evade the ubiquitous Type I DNA restriction systems and thereby assist the spread of resistance genes in bacterial populations. As such, ardA contributes to a major healthcare problem. We have solved the structure of the ArdA protein from the conjugative transposon Tn916 and find that it has a novel extremely elongated curved cylindrical structure with defined helical grooves. The high density of aspartate and glutamate residues on the surface follow a helical pattern and the whole protein mimics a 42-base pair stretch of B-form DNA making ArdA by far the largest DNA mimic known. Each monomer of this dimeric structure comprises three alpha-beta domains, each with a different fold. These domains have the same fold as previously determined proteins possessing entirely different functions. This DNA mimicry explains how ArdA can bind and inhibit the Type I restriction enzymes and we demonstrate that 6 different ardA from pathogenic bacteria can function in Escherichia coli hosting a range of different Type I restriction systems.

Indexed as

Molecular MimicryAmino Acid SequenceBacterial ProteinsCrystallography, X-RayDeoxyribonucleases, Type I Site-SpecificDimerizationDNADNA Restriction-Modification EnzymesDrug Resistance, BacterialGenome, BacterialModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidSite-Specific DNA-Methyltransferase (Adenine-Specific)Bacterial ProteinsDeoxyribonucleases, Type I Site-SpecificDNADNA modification methylase EcoKIDNA Restriction-Modification EnzymesSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID19506028
PMCPMC2731889
OpenAlexW2114725566

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.