Modulation of H-NS transcriptional silencing by magnesium

Nucleic Acids Research
W Ryan WillFerric C Fang

Abstract

The bacterial histone-like protein H-NS silences AT-rich DNA, binding DNA as 'stiffened' filaments or 'bridged' intrastrand loops. The switch between these modes has been suggested to depend on the concentration of divalent cations, in particular Mg2+, with elevated Mg2+ concentrations associated with a transition to bridging. Here we demonstrate that the observed binding mode is a function of the local concentration of H-NS and its cognate binding sites, as well as the affinity of the interactions between them. Mg2+ does not control a binary switch between these two modes but rather modulates the affinity of this interaction, inhibiting the DNA-binding and silencing activity of H-NS in a continuous linear fashion. The direct relationship between conditions that favor stiffening and transcriptional silencing activity suggests that although both modes can occur in the cell, stiffening is the predominant mode of binding at silenced genes.

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Citations

Jan 1, 2019·Nucleic Acids Research·Umar F Shahul HameedStefan T Arold
Oct 24, 2020·Theory in Biosciences = Theorie in Den Biowissenschaften·Yoan Konto-Ghiorghi, Vic Norris

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Methods Mentioned

BETA
atomic force microscopy
footprinting
PCR
AFM
magnetic tweezer
light scattering

Software Mentioned

Virtual Footprint program

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