Structural and Binding Properties of Dps - A Nucleoid Associated Protein.

ABSTRACT: Prokaryotic chromosomal DNA is compacted and protected by nucleoid-associated proteins (NAPs). Among these, the DNA-binding proteins from starved cells (Dps) combine ferroxidase activity with nonspecific DNA binding to form dodecameric assemblies that condense and safeguard the genome under stress. Here, we present an integrated structural and biophysical analysis of Escherichia coli (E. coli) Dps across a pH range from 3 to 11, combining (i) single-particle cryo-EM reconstructions at ~1.75 Å resolution, (ii) adaptive Poisson-Boltzmann electrostatic modelling, (iii) electrophoretic mobility shift assays (EMSAs) on a 448 bp DNA fragment, and (iv) cryo-electron tomography (cryo-ET) of Dps-DNA assemblies. Through this analysis, we show that (1) the canonical ferritin-like fold i

SUBMITTER: Gaines M 

PROVIDER: S-EPMC12642551 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature