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Updated: Sep 30, 2026

Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin
Sabine Reindel1, Stefan Anemüller, Andrzej Sawaryn
1Isotopenlabor TNF, Medizinische Universität zu Lübeck, Ratzeburger Allee 160, Lübeck, Germany.
Abstract:
An iron-rich protein, DpsA(Hsal), was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an alpha-helical contribution of 60%. The UV/VIS spectrum provides no evidence for the presence of heme groups. This protein exhibits features of a non-heme type bacterial ferritin (Ftn) although it shares only little sequence homology with Ftn. Molecular modelling disclosed a high structural similarity to E. coli Dps.
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