Antirestriction Protein ArdB (R64) Interacts with DNA
A. A. KudryavtsevaMoscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141707, Russia. [email protected]I.S. OkhrimenkoMoscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141707, RussiaV. S. DidinaMoscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141707, RussiaG. B. ZavilgelskyState Research Institute of Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center, Moscow, 117545, RussiaИ. В. МануховMoscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141707, Russia
2020en
ABI
Annotatsiya
The antirestriction ArdB protein inhibits the endonuclease activity of type I restriction/modification (RM) systems in vivo; however, the mechanism of inhibition remains unknown. In this study, we showed that recombinant ArdB from Escherichia coli cells co-purified with DNA. When overexpressed in E. coli cells, a portion of ArdB protein formed insoluble DNA-free aggregates. Only native ArdB, but not the ArdBAD141 mutant lacking the antirestriction activity, co-purified with DNA upon anion-exchange and affinity chromatography or total DNA isolation from formaldehyde-treated cells. These observations confirm the hypothesis that ArdB blocks DNA translocation via the R subunits of the R2M2S complex of type I RM enzymes.
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