DNA Binding Protein-7 (DBP-7), human recombinant

DNA Binding Protein-7 (DBP-7) is a N-terminal His-tagged recombinant protein and a member of the Sso7d family of small, abundant, non-specific DNA-binding proteins from the hyperthermophilic Archea Sulfolobus. The 7-kDa protein from Sulfolobus spp. consists of a five stranded, incomplete β-barrel capped at the opening by a C-terminal α-helix; they bind to the minor groove of a DNA duplex via the triple-stranded β-sheet. The topology of the Sulfolobus 7-kDa proteins was found to be similar to that of chromatin organization modifier (chromo) domains and eukaryotic SH3 domains, which are involved in protein–protein interactions. In vitro studies have shown that DBP-7 promotes the annealing of complementary DNA strands, induces negative supercoiling and chaperones the disassembly and renaturation of protein aggregates in an ATP hydrolysis-dependent manner.