van der Maarel, JRC, Guttula, D, Arluison, V, Egelhaaf, SU, Grillo, I and Forsyth, VT (2016) Structure of the H-NS-DNA nucleoprotein complex. Soft Matter, 12 (15). 3636 - 3642. ISSN 1744-6848

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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.

Item Type: Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Natural Sciences > School of Physical and Geographical Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 16 Nov 2016 12:20
Last Modified: 16 Nov 2016 12:20

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