Dps binds and protects DNA in starved <i>Escherichia coli</i> with minimal effect on chromosome accessibility, dynamics and organisation.

ABSTRACT: Dps is the most abundant nucleoid-associated protein in starved Escherichia coli with ~180,000 copies per cell. Dps binds DNA and oxidises iron, facilitating survival in harsh environments. Dps-DNA complexes can form crystalline structures, leading to the proposed model that Dps reorganises the starved E. coli nucleoid into a compact liquid crystal, slowing chromosome dynamics and limiting access of other proteins to DNA. In this work, we directly tested this model using live-cell super-resolution microscopy and Hi-C analysis. We found that after 96 h of starvation, Dps compacts the nucleoid and increases short-range DNA-DNA interactions, but does not affect chromosome accessibility to large protein nanocages or small restriction enzymes. We also report that chromosome dynami

SUBMITTER: McCarthy LA 

PROVIDER: S-EPMC12425006 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature