ArticleThe Journal of biological chemistry2015
A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- YmoA functions as a molecular stress sensor in Yersinia.Communications biology · 2025Article
- Article
- 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
- Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS.Nucleic acids research · 2024Article
- Repression by the H-NS/YmoA histone-like protein complex enables IscR dependent regulation of the Yersinia T3SS.PLoS genetics · 2022Article
- Novel anti-repression mechanism of H-NS proteins by a phage protein.Nucleic acids research · 2021Article
- A binding cooperativity switch driven by synergistic structural swelling of an osmo-regulatory protein pair.Nature communications · 2019Article
- H-NS uses an autoinhibitory conformational switch for environment-controlled gene silencing.Nucleic acids research · 2019Article
- Switching Protein Conformational Substates by Protonation and Mutation.The journal of physical chemistry. B · 2018Article
- Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation.The Journal of biological chemistry · 2018Article
- Tuning the Continuum of Structural States in the Native Ensemble of a Regulatory Protein.The journal of physical chemistry letters · 2017Article
- Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly.Nucleic acids research · 2017Article
- An oxygen-sensitive toxin-antitoxin system.Nature communications · 2016Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Hha/YmoA nucleoid-associated proteins help selectively silence horizontally acquired genetic material, including pathogenicity and antibiotic resistance genes and their maintenance in the absence of selective pressure. Members of the Hha family contribute to gene silencing by binding to the N-terminal dimerization domain of H-NS and modifying its selectivity. Hha-like proteins and the H-NS N-terminal domain are unusually rich in charged residues, and their interaction is mostly electrostatic-driven but, nonetheless, highly selective. The NMR-based structural model of the complex between Hha/YmoA and the H-NS N-terminal dimerization domain reveals that the origin of the selectivity is the formation of a three-protein charge zipper with interdigitated complementary charged residues from Hha and the two units of the H-NS dimer. The free form of YmoA shows collective microsecond-millisecond dynamics that can by measured by NMR relaxation dispersion experiments and shows a linear dependence with the salt concentration. The number of residues sensing the collective dynamics and the population of the minor form increased in the presence of H-NS. Additionally, a single residue mutation in YmoA (D43N) abolished H-NS binding and the dynamics of the apo-form, suggesting the dynamics and binding are functionally related.
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