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- W64879171 abstract "Dps (DNA protection during starvation) proteins play a significant role in the protection of prokaryotic macromolecules from damage by reactive oxygen species. Unlike other Dps homologs that protect DNA by a combination of DNA binding and sequestration of ferrous iron, Dps-1 from the radiation-resistant Deinococcus radiodurans fails to protect DNA from hydroxyl radical mediated degradation through a mechanism suggested to involve continuous release of iron from the protein core. Dps-1 also has a long lysine-rich N-terminal extension. In the crystal structure of Dps-1, the first ~30 N-terminal residues are invisible owing to disorder and the remaining ~24 residues form a loop that harbors a novel metal binding site. We show here that deletion of the flexible N-terminal obliterates DNA/Dps-1 interaction. Surprisingly, deletion of the entire N-terminus not only impaired DNA binding but also abolished dodecameric assembly of the protein. EMSA using DNA modified with major/minor groove reagents showed that Dps-1 interacts through the DNA major groove. DNA cyclization assays show that Dps-1 does not wrap DNA. DNA binding affinity decreases significantly with a reduction in duplex length from 26 bp to 18 bp, indicating optimal interactions with a duplex long enough to extend across the ~90Å face of the dodecamer. The mode of DNA interaction is consistent with the formation of stacked layers that results in DNA compaction." @default.
- W64879171 created "2016-06-24" @default.
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- W64879171 date "2007-04-01" @default.
- W64879171 modified "2023-09-30" @default.
- W64879171 title "The N‐terminal extension of Dps‐1 from Deinococcus radiodurans is required for assembly of the dodecamer as well as for DNA binding" @default.
- W64879171 doi "https://doi.org/10.1096/fasebj.21.5.a660-d" @default.
- W64879171 hasPublicationYear "2007" @default.
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