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Updated: Jul 15, 2025
12:41
Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
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Dps Functions as a Key Player in Bacterial Iron Homeostasis
Sunanda Margrett Williams1, Dipankar Chatterji2
1Institute of Structural and Molecular Biology, Birkbeck, University of London, Malet Street, London WC1E 7HX, United Kingdom.
ACS Omega
|October 2, 2023
Summary
DNA binding proteins under starvation (Dps) are prokaryotic iron storage proteins. This review highlights their role in iron homeostasis, DNA protection, and potential as an iron donor for iron-sulfur clusters.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Iron is essential for numerous cellular processes, including respiration and gene regulation.
- Maintaining iron in a safe, accessible form is critical for cellular function.
- DNA binding proteins under starvation (Dps) are ferritin-like proteins found in prokaryotes, storing iron and protecting DNA.
Purpose of the Study:
- To review the biochemical and structural properties of Dps, focusing on iron storage and ferroxidation.
- To examine the potential role of Dps as an iron donor for iron-sulfur clusters.
Main Methods:
- Biochemical studies
- Structural studies
- Literature review
Main Results:
- Dps efficiently store iron within their protein shells.
- Dps exhibit ferroxidation capabilities.
- Dps may serve as an iron donor for iron-sulfur cluster biosynthesis.
Conclusions:
- Dps are multifunctional proteins crucial for iron homeostasis in prokaryotes.
- Their roles extend to DNA protection and potentially iron delivery for essential metalloproteins.
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