Abstract
DNA mimicking ArdA anti-restriction proteins specifically inhibit restriction (endonuclease) activity of the type I restriction-modification (RM) system. An ArdA monomer is comprised of three α-β domains (the N-domain, Central domain, and C-domain), each with a different fold. Here we describe an alignment of the amino acid (a.a.) sequences of the ArdA with a conserved 20-a.a. motif in the N domain. The N domains of ArdA proteins of the Gram-positive bacteria Arthrobacter sp. and Bifidobacterium longum, and the Gram-negative bacteria Pseudomonas plecoglossicida are capable of inhibiting the repressive activity of the H-NS global silencer protein in Escherichia coli cells. The presence of the H-NS inhibiting N domain in the ArdA structure enables horizontal gene transfer by mobile elements, including conjugative plasmids and transposons. Specifically, it aids in overcoming intercellular restriction barriers, allowing faster adaption to the genome context of the recipient bacterium.
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ACKNOWLEDGMENTS
The authors are grateful to the staff of the NRC Kurchatov Institute, Sergei Rastorguev and Aleksei Kozhenkov, for their assistance in genome-wide sequencing of bacteria and the search for ardA nucleotide gene sequences.
Funding
This work was supported by the Russian Foundation for Basic Research (project no. 19-04-00495).
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The authors declare they have no conflict of interest. The study contains no research using humans or animals as objects of study.
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Abbreviations: a.a., amino acid residue (with number).
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Melkina, O.E., Zavilgelsky, G.B. N-Domain of ArdA Antirestriction Proteins Inhibits the Repression Activity of the Histone-Like H-NS Protein. Mol Biol 55, 424–431 (2021). https://doi.org/10.1134/S0026893321020266
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DOI: https://doi.org/10.1134/S0026893321020266