Integration host factor bends and bridges DNA in a multiplicity of binding modes with varying specificity.

ABSTRACT: Nucleoid-associated proteins (NAPs) are crucial in organizing prokaryotic DNA and regulating genes. Vital to these activities are complex nucleoprotein structures, however, how these form remains unclear. Integration host factor (IHF) is an Escherichia coli NAP that creates very sharp bends in DNA at sequences relevant to several functions including transcription and recombination, and is also responsible for general DNA compaction when bound non-specifically. We show that IHF-DNA structural multimodality is more elaborate than previously thought, and provide insights into how this drives mechanical switching towards strongly bent DNA. Using single-molecule atomic force microscopy and atomic molecular dynamics simulations we find three binding modes in roughly equal proportions: 'associate

SUBMITTER: Yoshua SB 

PROVIDER: S-EPMC8421141 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature