ArticleNucleic acids research2020
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 45 citations in OpenAlex.
- Bacterial 3D genome architecture: organization, regulation, and synthetic biology applications.Genome biology · 2026Review
- Cyclic-di-GMP interferes with DNA-MucR-DNA bridging to derepress genes targeted by the xenogeneic silencer MucR.Nucleic acids research · 2025Article
- Metagenomic approaches for studying ubiquitous yet diverse nucleoid associated proteins in microbial communities: challenges and advances.World journal of microbiology & biotechnology · 2025Review
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Post-translational modifications of the nucleoid protein H-NS: sites, mechanisms, and regulatory cues.FEMS microbiology reviews · 2025Review
- Oligomerization-mediated phase separation in the nucleoid-associated sensory protein H-NS is controlled by ambient cues.Protein science : a publication of the Protein Society · 2025Article
- High-throughput single-molecule nanofluidic studies onQRB discovery · 2025Article
- Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS.Nucleic acids research · 2024Article
- Lysine acetylation regulates the AT-rich DNA possession ability of H-NS.Nucleic acids research · 2024Article
- Quantitative Determination of DNA Bridging Efficiency of Chromatin Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Tethered Particle Motion Analysis of DNA-Binding Properties of Architectural Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- c-di-GMP inhibits the DNA binding activity of H-NS in Salmonella.Nature communications · 2023Article
- The environmentally-regulated interplay between local three-dimensional chromatin organisation and transcription of proVWX in E. coli.Nature communications · 2023Article
- DNA-bridging by an archaeal histone variant via a unique tetramerisation interface.Communications biology · 2023Article
- The Xenogeneic Silencer Histone-Like Nucleoid-Structuring Protein Mediates the Temperature and Salinity-Dependent Regulation of the Type III Secretion System 2 in Vibrio parahaemolyticus.Journal of bacteriology · 2023Article
- The B. subtilis Rok protein is an atypical H-NS-like protein irresponsive to physico-chemical cues.Nucleic acids research · 2022Article
- System-Wide Analysis of the GATC-Binding Nucleoid-Associated Protein Gbn and Its Impact onmSystems · 2022Article
- Bacterial H-NS contacts DNA at the same irregularly spaced sites in both bridged and hemi-sequestered linear filaments.iScience · 2022Article
- Special Issue: Role of Bacterial Chromatin in Environmental Sensing, Adaptation and Evolution.Microorganisms · 2021Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
H-NS proteins act as osmotic sensors translating changes in osmolarity into altered DNA binding properties, thus, regulating enterobacterial genome organization and genes transcription. The molecular mechanism underlying the switching process and its conservation among H-NS family members remains elusive. Here, we focus on the H-NS family protein MvaT from Pseudomonas aeruginosa and demonstrate experimentally that its protomer exists in two different conformations, corresponding to two different functional states. In the half-opened state (dominant at low salt) the protein forms filaments along DNA, in the fully opened state (dominant at high salt) the protein bridges DNA. This switching is a direct effect of ionic strength on electrostatic interactions between the oppositely charged DNA binding and N-terminal domains of MvaT. The asymmetric charge distribution and intramolecular interactions are conserved among the H-NS family of proteins. Therefore, our study establishes a general paradigm for the molecular mechanistic basis of the osmosensitivity of H-NS proteins.
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