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

TitleArdA proteins from different mobile genetic elements can bind to the EcoKI Type I DNA methyltransferase of E. coli K12.
Publication TypeJournal Article
Year of Publication2014
AuthorsChen K, Reuter M, Sanghvi B, Roberts GA, Cooper LP, Tilling M, Blakely GW, Dryden DTF
JournalBiochim Biophys Acta
Volume1844
Issue3
Pagination505-11
Date Published2014 Mar
ISSN0006-3002
KeywordsChromatography, Gel, Circular Dichroism, Escherichia coli K12, Escherichia coli Proteins, Interspersed Repetitive Sequences, Models, Molecular, Protein Binding, Protein Denaturation, Protein Structure, Secondary, Repressor Proteins, Site-Specific DNA-Methyltransferase (Adenine-Specific)
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.

DOI10.1016/j.bbapap.2013.12.008
Alternate JournalBiochim. Biophys. Acta
PubMed ID24368349
PubMed Central IDPMC3969726
Grant List090288/Z/09/ZA / / Wellcome Trust / United Kingdom
BB/C511599/1 / / Biotechnology and Biological Sciences Research Council / United Kingdom
BB/D001870/1 / / Biotechnology and Biological Sciences Research Council / United Kingdom
GR080463MA / / Wellcome Trust / United Kingdom
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