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Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance
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dc.contributor.author | McMahon, Stephen A. | |
dc.contributor.author | Roberts, Gareth A. | |
dc.contributor.author | Johnson, Kenneth A. | |
dc.contributor.author | Cooper, Laurie P. | |
dc.contributor.author | Liu, Huanting | |
dc.contributor.author | White, John H. | |
dc.contributor.author | Carter, Lester G. | |
dc.contributor.author | Sanghvi, Bansi | |
dc.contributor.author | Oke, Muse | |
dc.contributor.author | Walkinshaw, Malcolm D. | |
dc.contributor.author | Blakely, Garry W. | |
dc.contributor.author | Naismith, James Henderson | |
dc.contributor.author | Dryden, David T. F. | |
dc.date.accessioned | 2013-12-05T13:01:08Z | |
dc.date.available | 2013-12-05T13:01:08Z | |
dc.date.issued | 2009-08 | |
dc.identifier.citation | McMahon , S A , Roberts , G A , Johnson , K A , Cooper , L P , Liu , H , White , J H , Carter , L G , Sanghvi , B , Oke , M , Walkinshaw , M D , Blakely , G W , Naismith , J H & Dryden , D T F 2009 , ' Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance ' , Nucleic Acids Research , vol. 37 , no. 15 , pp. 4887-4897 . https://doi.org/10.1093/nar/gkp478 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | PURE: 1679723 | |
dc.identifier.other | PURE UUID: 36b2bf22-05ba-4b58-9828-4848ae9a5c14 | |
dc.identifier.other | WOS: 000270016400001 | |
dc.identifier.other | Scopus: 69849087746 | |
dc.identifier.uri | https://hdl.handle.net/10023/4276 | |
dc.description.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 alphabeta 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. | |
dc.format.extent | 11 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.rights | © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. | en |
dc.subject | CONJUGATIVE TRANSPOSON TN916 | en |
dc.subject | ANTIRESTRICTION PROTEIN | en |
dc.subject | MODIFICATION SYSTEM | en |
dc.subject | ESCHERICHIA-COLI | en |
dc.subject | STAPHYLOCOCCUS-AUREUS | en |
dc.subject | BACTERIOPHAGE T7 | en |
dc.subject | RESTRICTION/MODIFICATION ENZYME | en |
dc.subject | MYCOBACTERIUM-TUBERCULOSIS | en |
dc.subject | ENTEROCOCCUS-FAECALIS | en |
dc.subject | SDG 3 - Good Health and Well-being | en |
dc.title | Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance | en |
dc.type | Journal article | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.identifier.doi | https://doi.org/10.1093/nar/gkp478 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | http://www.scopus.com/inward/record.url?scp=69849087746&partnerID=8YFLogxK | en |
dc.identifier.url | http://ukpmc.ac.uk/abstract/MED/19506028 | en |
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