ArticleNucleic acids research2025
Amyloid-like DNA bridging: a new mode of DNA shaping.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A modular framework for automated segmentation and analysis of AFM imaging of chromatin organization.Nucleic acids research · 2026Article
- Uncovering a previously unknown function of polyphosphate in polyadenylated RNA-induced amyloidogenesis of Hfq.The FEBS journal · 2026Article
- DNA methylation enhances cooperative disentanglement by the Hfq nucleoid-associated protein.European biophysics journal : EBJ · 2026Article
- Reversible DNA condensation drives natural transformation.Nature communications · 2026Article
- DNA Modulates Structural Transitions and Oligomerization Kinetics of the Functional Amyloid CRES.Journal of the American Chemical Society · 2026Article
- Inelastic Neutron Scattering: Prospects for Measuring Atomic Vibrations of Nucleic Acids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Dental plaque biofilm transforms host-derived βBiofilm · 2025Article
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- Does the Hfq Protein Contribute to RNA Cargo Translocation into Bacterial Outer Membrane Vesicles?Pathogens (Basel, Switzerland) · 2025Article
- Review
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Authors and funding
14 authors.
Funding
Abstract
All organisms depend on specific proteins to compact and organize their genomes. In eukaryotes, histones fulfil this role, while bacterial chromosomes are shaped by nucleoid-associated proteins (NAPs). Among its pleiotropic functions, the NAP Hfq plays a pivotal role in bacterial genome organization. In this study, we characterized the structure of the C-terminal extension of Hfq, which mediates chromosomal compaction, in its DNA-bound state. Using an integrative approach that combined transmission electron microscopy, neutron scattering, site-directed mutagenesis, and molecular modeling, we identified an amyloid module formed by the C-terminal region of Hfq. This module uniquely bridges and compacts six DNA molecules, marking the first documented instance of an amyloid structure with DNA-bridging properties. Our findings redefine the functional landscape of amyloids, linking them to genome architecture and gene regulation. This result suggests that amyloid-DNA interactions may represent a conserved mechanism across biological systems, with profound implications for understanding genome organization and the regulation of gene expression in both prokaryotes and eukaryotes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.