%0 Journal Article %A Das, Anubrata D. %A Misra, Hari S. %T Characterization of DRA0282 from Deinococcus radiodurans for its role in bacterial resistance to DNA damage %D 2011 %J Microbiology, %V 157 %N 8 %P 2196-2205 %@ 1465-2080 %R https://doi.org/10.1099/mic.0.040436-0 %I Microbiology Society, %X DRA0282, a hypothetical protein, was found in a pool of nucleotide-binding proteins in Deinococcus radiodurans cells recovering from gamma radiation stress. This pool exhibited an unusual inhibition of nuclease activity by ATP. The N terminus of DRA0282 showed similarity to human Ku80 homologues, while the C terminus showed no similarities to known proteins. The recombinant protein required Mn2+ for its interaction with DNA and protected dsDNA from exonuclease III degradation. The binding of the protein to supercoiled DNA with a K d of ~2.93 nM was nearly 20-fold stronger than its binding to ssDNA and nearly 67-fold stronger than its binding to linear dsDNA. Escherichia coli cells expressing DRA0282 showed a RecA-dependent enhancement of UV and gamma radiation tolerance. The ΔdrA0282 mutant of D. radiodurans showed a dose-dependent response to gamma radiation. At 14 kGy, the ΔdrA0282 mutant showed nearly 10-fold less survival, while at this dose both pprA : : catΔdrA0282 and pprA : : cat mutants were nearly 100-fold more sensitive than the wild-type. These results suggested that DRA0282 is a DNA-binding protein with a preference for superhelical DNA, and that it plays a role in bacterial resistance to DNA damage through a pathway in which PprA perhaps plays a dominant role in D. radiodurans. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.040436-0