Direct visualization of the effect of DNA structure and ionic conditions on HU-DNA interactions.

ABSTRACT: Architectural DNA-binding proteins are involved in many important DNA transactions by virtue of their ability to change DNA conformation. Histone-like protein from E. coli strain U93, HU, is one of the most studied bacterial architectural DNA-binding proteins. Nevertheless, there is still a limited understanding of how the interactions between HU and DNA are affected by ionic conditions and the structure of DNA. Here, using optical tweezers in combination with fluorescent confocal imaging, we investigated how ionic conditions affect the interaction between HU and DNA. We directly visualized the binding and the diffusion of fluorescently labelled HU dimers on DNA. HU binds with high affinity and exhibits low mobility on the DNA in the absence of Mg²⁺; it moves 30-times faster and

SUBMITTER: Lin SN 

PROVIDER: S-EPMC8446073 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature