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• W1690152478 endingPage "4327" @default.
• W1690152478 startingPage "4307" @default.
• W1690152478 abstract "The DNA binding proteins from starved cells from Deinococcus radiodurans, Dps1-DR2263 and Dps2-DRB0092, have a common overall structure of hollow spherical dodecamers. Their involvement in the homeostasis of intracellular metal and DNA protection was addressed. Our results show that DrDps proteins are able to oxidize ferrous to ferric iron by oxygen or hydrogen peroxide. The iron stored inside the hollow sphere cavity is fully released. Furthermore, these proteins are able to store and release manganese, suggesting they can play a role in manganese homeostasis as well. The interaction of DrDps with DNA was also addressed. Even though DrDps1 binds both linear and coiled DNA, DrDps2 preferentially binds to coiled DNA, forming different protein-DNA complexes, as clearly shown by atomic force microscopy. DrDps1 (dimer and dodecamer) and DrDps2 can protect DNA against reactive oxygen species, although the protection occurs at different Fe to protein ratios. The difference between DrDps could be the result of the DrDps1 higher iron oxidation rate in the presence of hydrogen peroxide and its higher affinity to bind DNA than in DrDps2. Using cellular extracts obtained from D. radiodurans cultures, we showed that DrDps1 oligomers observed in in vitro conditions are also present in vivo. This indicates that DrDps1 has a structural dynamic plasticity that allows its oligomeric state to change between dimer, trimer and dodecamer. This in turn suggests the existence of a regulation mechanism that modulates the oligomer equilibrium and is dependent on growth stages and environmental conditions." @default.
• W1690152478 created "2016-06-24" @default.
• W1690152478 creator A5005037997 @default.
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• W1690152478 creator A5086013075 @default.
• W1690152478 date "2015-09-18" @default.
• W1690152478 modified "2023-10-15" @default.
• W1690152478 title "Dps from<i>Deinococcus radiodurans</i>: oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage" @default.
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• W1690152478 doi "https://doi.org/10.1111/febs.13420" @default.
• W1690152478 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26290287" @default.
• W1690152478 hasPublicationYear "2015" @default.
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