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Bridging DNA contacts allow Dps from E. coli to condense DNA
Sneha Shahu1, Natalia Vtyurina1,2,3, Moumita Das3
1Department of Biochemistry, Indian Institute of Science, Bangalore, India.
Biorxiv : the Preprint Server for Biology
|February 8, 2024
Summary
DNA-binding protein from starved cells (Dps) preferentially binds supercoiled DNA, forming stable complexes. Bridging DNA contacts are key for Dps nucleation and stabilization during bacterial stress responses.
Area of Science:
- Microbiology
- Biochemistry
- Structural Biology
Background:
- DNA-binding protein from starved cells (Dps) is vital for bacterial survival under stress.
- Dps forms nucleoid-associated biomolecular condensates with DNA in vivo.
- Purified Dps rapidly forms large complexes with DNA in vitro, but nucleation mechanisms are unclear.
Approach:
- Investigated the influence of DNA topology on Dps-DNA complex formation.
- Utilized in vitro assays to observe Dps-DNA interactions.
- Analyzed the role of DNA supercoiling and bridging contacts.
Key Points:
- DNA supercoils serve as preferred templates for Dps condensate nucleation.
- Bridging DNA contacts significantly facilitate Dps complex nucleation.
- Dps shows low affinity for relaxed, linear DNA before condensation.
- Condensed DNA-DNA complexes are stable, even without free Dps.
Conclusions:
- DNA topology, particularly supercoiling and bridging contacts, is critical for Dps nucleation.
- Bridging contacts are essential for both nucleating and stabilizing Dps-DNA complexes.
- Understanding these interactions provides insight into bacterial stress adaptation mechanisms.
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