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Updated: Dec 26, 2025

Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer
Takuo Minato1,2, Takamasa Teramoto3, Yoshimitsu Kakuta3,4
1Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.
Abstract:
The DNA-binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X-ray crystallographic analysis revealed that TlDps1 possessed His-type ferroxidase centers within the cavity and unique metal-binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability.
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