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Issue 15, 2016
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Structure of the H-NS–DNA nucleoprotein complex

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Abstract

Nucleoid associated proteins (NAPs) play a key role in the compaction and expression of the prokaryotic genome. Here we report the organisation of a major NAP, the protein H-NS on a double stranded DNA fragment. For this purpose we have carried out a small angle neutron scattering study in conjunction with contrast variation to obtain the contributions to the scattering (structure factors) from DNA and H-NS. The H-NS structure factor agrees with a heterogeneous, two-state binding model with sections of the DNA duplex surrounded by protein and other sections having protein bound to the major groove. In the presence of magnesium chloride, we observed a structural rearrangement through a decrease in cross-sectional diameter of the nucleoprotein complex and an increase in fraction of major groove bound H-NS. The two observed binding modes and their modulation by magnesium ions provide a structural basis for H-NS-mediated genome organisation and expression regulation.

Graphical abstract: Structure of the H-NS–DNA nucleoprotein complex

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Supplementary files

Article information


Submitted
21 Dec 2015
Accepted
09 Mar 2016
First published
09 Mar 2016

This article is Open Access

Soft Matter, 2016,12, 3636-3642
Article type
Paper

Structure of the H-NS–DNA nucleoprotein complex

J. R. C. van der Maarel, D. Guttula, V. Arluison, S. U. Egelhaaf, I. Grillo and V. T. Forsyth, Soft Matter, 2016, 12, 3636
DOI: 10.1039/C5SM03076E

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