ArticleInternational journal of molecular sciences2025
The Dps Protein Protects
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Investigation of the Mechanisms of Transition of Gram-Negative Bacterial Cells into Induced Anabiosis Using Computational Methods of Classical Molecular Dynamics.Microorganisms · 2026Article
- Dps binds and protects DNA in starved Escherichia coli with minimal effect on chromosome accessibility, dynamics, and organization.Nucleic acids research · 2026Article
- Dps binds and protects DNA in starvedbioRxiv : the preprint server for biology · 2025Article
- Structural and Binding Properties of Dps - A Nucleoid Associated Protein.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Dps protein is the major DNA-binding protein of prokaryotes, which protects DNA during starvation by forming a crystalline complex. The structure of such an intracellular DNA-Dps complex is still unknown. However, the phenomenon of a decrease in the size of the Dps protein from 90 Å to 69-75 Å during the formation of a complex with DNA has been repeatedly observed, and no explanation has been given. In this work, we show that during the formation of intracellular DNA-Dps crystals, the protein transitions to another oligomeric form: from a dodecameric (of 12 monomers), which has an almost spherical shape with a diameter of 90 Å, to a trimeric (of three monomers), which has a shape close to a torus-like structure with a diameter of 70 Å and a height of 40 Å. The trimer model was obtained through the molecular dynamic modeling of the interaction of the three monomers of the Dps protein. Placement of the obtained trimer in the electron density of in vitro DNA-Dps crystal allowed for the determination of the lattice parameters of the studied crystal. This crystal model was in good agreement with the SAXS data obtained from intracellular crystals of 2-day-old
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