Bridging DNA contacts allow Dps from E. coli to condense DNA.

Autor:	Shahu S; Department of Biochemistry, Indian Institute of Science, Bangalore, India., Vtyurina N, Das M; School of Physics and Astronomy, Rochester Institute of Technology, Rochester, NY 14623, USA., Meyer AS; Department of Biology, University of Rochester, Rochester, NY 14627, USA., Ganji M; Department of Biochemistry, Indian Institute of Science, Bangalore, India., Abbondanzieri EA; Department of Biology, University of Rochester, Rochester, NY 14627, USA.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2024 May 08; Vol. 52 (8), pp. 4456-4465.
DOI:	10.1093/nar/gkae223
Abstrakt:	The DNA-binding protein from starved cells (Dps) plays a crucial role in maintaining bacterial cell viability during periods of stress. Dps is a nucleoid-associated protein that interacts with DNA to create biomolecular condensates in live bacteria. Purified Dps protein can also rapidly form large complexes when combined with DNA in vitro. However, the mechanism that allows these complexes to nucleate on DNA remains unclear. Here, we examine how DNA topology influences the formation of Dps-DNA complexes. We find that DNA supercoils offer the most preferred template for the nucleation of condensed Dps structures. More generally, bridging contacts between different regions of DNA can facilitate the nucleation of condensed Dps structures. In contrast, Dps shows little affinity for stretched linear DNA before it is relaxed. Once DNA is condensed, Dps forms a stable complex that can form inter-strand contacts with nearby DNA, even without free Dps present in solution. Taken together, our results establish the important role played by bridging contacts between DNA strands in nucleating and stabilizing Dps complexes. (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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