Please use this identifier to cite or link to this item: https://doi.org/10.1039/c5sm03076e
Title: Structure of the H-NS-DNA nucleoprotein complex
Authors: Van Der Maarel, J.R.C 
Guttula, D 
Arluison, V
Egelhaaf, S.U
Grillo, I
Forsyth, V.T
Keywords: Amorphous alloys
Binding energy
Bins
Genes
Magnesium
Metal ions
Metallic glass
Neutron scattering
Nucleic acids
Proteins
Contrast variation
Cross sectional diameters
Double stranded DNA
Expression regulation
Magnesium chlorides
Prokaryotic genomes
Structural rearrangement
Structure factors
DNA
bacterial protein
DNA
DNA binding protein
H-NS protein, bacteria
nucleoprotein
protein binding
chemistry
conformation
genomics
metabolism
molecular model
protein secondary structure
Bacterial Proteins
DNA
DNA-Binding Proteins
Genomics
Models, Molecular
Nucleic Acid Conformation
Nucleoproteins
Protein Binding
Protein Structure, Secondary
Issue Date: 2016
Citation: Van Der Maarel, J.R.C, Guttula, D, Arluison, V, Egelhaaf, S.U, Grillo, I, Forsyth, V.T (2016). Structure of the H-NS-DNA nucleoprotein complex. Soft Matter 12 (15) : 3636-3642. ScholarBank@NUS Repository. https://doi.org/10.1039/c5sm03076e
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. © The Royal Society of Chemistry 2016.
Source Title: Soft Matter
URI: https://scholarbank.nus.edu.sg/handle/10635/174095
ISSN: 1744683X
DOI: 10.1039/c5sm03076e
Appears in Collections:Elements
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