Role of Salt Valency in the Switch of H-NS Proteins between DNA-Bridging and DNA-Stiffening Modes (Q88166208)

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21 March 2020

title

Role of Salt Valency in the Switch of H-NS Proteins between DNA-Bridging and DNA-Stiffening Modes (English)

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1

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publication date

23 March 2018

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volume

114

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issue

10

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page(s)

2317-2325

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Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity

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cites work

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Counterion-induced condensation of deoxyribonucleic acid. A light-scattering study

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Ion effects on ligand-nucleic acid interactions

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Thermodynamics of single-stranded RNA binding to oligolysines containing tryptophan

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Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids

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Enthalpy-entropy compensations in drug-DNA binding studies

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Pentalysine-deoxyribonucleic acid interactions: a model for the general effects of ion concentrations on the interactions of proteins with nucleic acids.

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Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria.

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Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid

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Multimeric Self-assembly Equilibria Involving the Histone-like Protein H-NS: A THERMODYNAMIC STUDY

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Oligomerization of the chromatin-structuring protein H-NS.

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H-NS mediated compaction of DNA visualised by atomic force microscopy

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H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein

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The H-NS dimerization domain defines a new fold contributing to DNA recognition

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Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor

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The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin

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H-NS is a part of a thermally controlled mechanism for bacterial gene regulation.

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H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing

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The Major Architects of Chromatin: Architectural Proteins in Bacteria, Archaea and Eukaryotes

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Description of nonspecific DNA-protein interaction and facilitated diffusion with a dynamical model

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A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes.

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Comparison of kinetic and dynamical models of DNA-protein interaction and facilitated diffusion

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H-NS forms a superhelical protein scaffold for DNA condensation

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Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins

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Theoretical Assessment of the Oligolysine Model for Ionic Interactions in Protein–DNA Complexes

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Gene silencing H-NS paralogue StpA forms a rigid protein filament along DNA that blocks DNA accessibility

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12 December 2020

Nucleoprotein filament formation is the structural basis for bacterial protein H-NS gene silencing

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The nucleoid-associated protein Dan organizes chromosomal DNA through rigid nucleoprotein filament formation in E. coli during anoxia

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A model of H-NS mediated compaction of bacterial DNA.

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Different thermodynamic signatures for DNA minor groove binding with changes in salt concentration and temperature

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Equilibration of complexes of DNA and H-NS proteins on charged surfaces: a coarse-grained model point of view.

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Bridged filaments of histone-like nucleoid structuring protein pause RNA polymerase and aid termination in bacteria

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Building bridges within the bacterial chromosome.

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Effect of H-NS on the elongation and compaction of single DNA molecules in a nanospace.

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Live-cell superresolution microscopy reveals the organization of RNA polymerase in the bacterial nucleoid

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Compaction of bacterial genomic DNA: clarifying the concepts

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Structure of the H-NS-DNA nucleoprotein complex.

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Coarse-Grained Model of the Demixing of DNA and Non-Binding Globular Macromolecules

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12 December 2020

Mechanism of environmentally driven conformational changes that modulate H-NS DNA-bridging activity

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12 December 2020

10.1016/J.BPJ.2018.02.030

Identifiers

DOI

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21 March 2020

0 references

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21 March 2020

PubMed publication ID

29576193

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