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Single‐stranded DNA binding protein (Ssb) of Deinococcus radiodurans  comprises N‐ and C‐terminal oligonucleotide/oligosaccharide binding (OB) folds connected by a beta hairpin connector. To assign functional roles to the individual OB folds, we generated three Ssb variants: Ssb N  (N‐terminal without connector), Ssb NC  (N‐terminal with connector) and Ssb C  (C‐terminal), each harboring one OB fold. Both Ssb N  and Ssb NC  displayed weak single‐stranded DNA (ssDNA) binding activity, compared to the full‐length Ssb (Ssb FL ). The level of ssDNA binding activity displayed by Ssb C  was intermediate between Ssb FL  and Ssb N . Ssb C  and Ssb FL  predominantly existed as homo‐dimers while Ssb NC /Ssb N  formed different oligomeric forms. In vitro , Ssb NC  or Ssb N  formed a binary complex with Ssb C  that displayed enhanced ssDNA binding activity. Unlike Ssb FL , Ssb variants were able to differentially modulate topoisomerase‐I activity, but failed to stimulate Deinococcal RecA‐promoted DNA strand exchange. The results suggest that the C‐terminal OB fold is primarily responsible for ssDNA binding. The N‐terminal OB fold binds weakly to ssDNA but is involved in multimerization.

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Functional roles of N‐terminal and C‐terminal domains in the overall activity of a novel single‐stranded DNA binding protein of Deinococcus radiodurans